|
Inhibitory concentration against purified penicillin-binding protein(PBP) 1bgamma of Escherichia coli
|
Escherichia coli
|
10.0
nM
|
|
Journal : J. Med. Chem.
Title : Synthesis and structure-activity relationship of (lactamylvinyl)cephalosporins exhibiting activity against staphylococci, pneumococci, and enterococci.
Year : 1996
Volume : 39
Issue : 9
First Page : 1864
Last Page : 1871
Authors : Heinze-Krauss I, Angehrn P, Guerry P, Hebeisen P, Hubschwerlen C, Kompis I, Page MG, Richter HG, Runtz V, Stalder H, Weiss U, Wei CC.
Abstract : The synthesis and structure-activity relationships of a new class of vinylcephalosporins substituted with a lactamyl residue are described. These compounds show excellent activity against enterococci and retain the broad spectrum activity of third-generation cephalosporins such as ceftriaxone.
|
In vitro binding affinity towards PBP2'' of Staphylococcus aureus using [14C]benzylpenicillin as radioligand
|
Staphylococcus aureus
|
430.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Synthesis and antibacterial activity of lipophilic carbapenems with anti-MRSA activity
Year : 1996
Volume : 6
Issue : 20
First Page : 2449
Last Page : 2454
Authors : Arnould JC, Illingworth RN, Nichols WW, Geoffrey Wilson R
|
Binding affinity against PBP2a receptor by competition analysis with [3H]benzylpenicillin using cell membrane fractions from the MRSA COL strain.
|
Staphylococcus aureus
|
100.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Dicationic 2-fluorenonylcarbapenems: potent anti-MRS agents with improved solubility and pharmacokinetic properties.
Year : 1999
Volume : 9
Issue : 22
First Page : 3225
Last Page : 3230
Authors : Greenlee ML, Laub JB, Rouen GP, DiNinno F, Hammond ML, Huber JL, Sundelof JG, Hammond GG.
Abstract : The synthesis and biological evaluation of a series of dicationic-substituted 2-fluorenonylcarbapenems is described. This class of compounds showed enhanced water solubility while maintaining potent activity against MRS. Introduction of a 1-beta-methyl substituent was found to improve pharmacokinetics.
|
Antibacterial activity expressed as binding to PBP 1a of Pseudomonas aeruginosa
|
Pseudomonas aeruginosa
|
300.0
nM
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Design and synthesis of bridged gamma-lactams as analogues of beta-lactam antibiotics.
Year : 2004
Volume : 14
Issue : 10
First Page : 2489
Last Page : 2492
Authors : Aszodi J, Rowlands DA, Mauvais P, Collette P, Bonnefoy A, Lampilas M.
Abstract : Anti-Bredt bridged bicyclo[3.2.1] gamma-lactams were designed as inhibitors of penicillin binding proteins (PBPs). The compounds were prepared by a carbenoid insertion into a lactam N-H bond. Their weak antibacterial activity could either be explained by a poor chemical stability or by unfavorable steric interactions of the methylene bridge of the gamma-lactam with the targeted enzymes.
|
Antibacterial activity expressed as binding to PBP 1b of Pseudomonas aeruginosa
|
Pseudomonas aeruginosa
|
600.0
nM
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Design and synthesis of bridged gamma-lactams as analogues of beta-lactam antibiotics.
Year : 2004
Volume : 14
Issue : 10
First Page : 2489
Last Page : 2492
Authors : Aszodi J, Rowlands DA, Mauvais P, Collette P, Bonnefoy A, Lampilas M.
Abstract : Anti-Bredt bridged bicyclo[3.2.1] gamma-lactams were designed as inhibitors of penicillin binding proteins (PBPs). The compounds were prepared by a carbenoid insertion into a lactam N-H bond. Their weak antibacterial activity could either be explained by a poor chemical stability or by unfavorable steric interactions of the methylene bridge of the gamma-lactam with the targeted enzymes.
|
Antibacterial activity expressed as binding to PBP 2 of Pseudomonas aeruginosa
|
Pseudomonas aeruginosa
|
600.0
nM
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Design and synthesis of bridged gamma-lactams as analogues of beta-lactam antibiotics.
Year : 2004
Volume : 14
Issue : 10
First Page : 2489
Last Page : 2492
Authors : Aszodi J, Rowlands DA, Mauvais P, Collette P, Bonnefoy A, Lampilas M.
Abstract : Anti-Bredt bridged bicyclo[3.2.1] gamma-lactams were designed as inhibitors of penicillin binding proteins (PBPs). The compounds were prepared by a carbenoid insertion into a lactam N-H bond. Their weak antibacterial activity could either be explained by a poor chemical stability or by unfavorable steric interactions of the methylene bridge of the gamma-lactam with the targeted enzymes.
|
Antibacterial activity expressed as binding to PBP 4 of Pseudomonas aeruginosa
|
Pseudomonas aeruginosa
|
100.0
nM
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Design and synthesis of bridged gamma-lactams as analogues of beta-lactam antibiotics.
Year : 2004
Volume : 14
Issue : 10
First Page : 2489
Last Page : 2492
Authors : Aszodi J, Rowlands DA, Mauvais P, Collette P, Bonnefoy A, Lampilas M.
Abstract : Anti-Bredt bridged bicyclo[3.2.1] gamma-lactams were designed as inhibitors of penicillin binding proteins (PBPs). The compounds were prepared by a carbenoid insertion into a lactam N-H bond. Their weak antibacterial activity could either be explained by a poor chemical stability or by unfavorable steric interactions of the methylene bridge of the gamma-lactam with the targeted enzymes.
|
Binding affinity towards Penicillin-binding protein 2a from homogeneous MRSA COL strain using [3H]-radioligand
|
Staphylococcus aureus
|
128.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Benzothiazolylthio carbapenems: potent anti-MRSA agents
Year : 1995
Volume : 5
Issue : 13
First Page : 1427
Last Page : 1432
Authors : Waddell ST, Ratcliffe RW, Szumiloski SP, Wildonger KJ, Wilkening RR, Blizzard TA, Huber J, Kohler J, Dorso K, Rose ES, Sundelof JG, Hammond GG
|
Compound was tested for its binding affinity towards Penicillin-binding protein 2a (PBP2a) using [13H]-benzylpenicillin
|
None
|
188.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Synthesis and activity of 2-(sulfonamido)methyl-carbapenems: discovery of a novel, anti-MRSA 1,8-naphthosultam pharmacophore.
Year : 1999
Volume : 9
Issue : 5
First Page : 673
Last Page : 678
Authors : Wilkening RR, Ratcliffe RW, Wildonger KJ, Cama LD, Dykstra KD, DiNinno FP, Blizzard TA, Hammond ML, Heck JV, Dorso KL, St Rose E, Kohler J, Hammond GG.
Abstract : A series of 1beta-methyl carbapenems substituted at the 2-position with lipophilic, acyclic and cyclic (sulfonamido)methyl groups was prepared and evaluated for activity against resistant gram-positive bacteria. From these studies, the 1,8-naphthosultamyl group emerged as a novel, PBP2a-binding, anti-MRSA pharmacophore worthy of further exploration.
|
Compound was tested for its binding affinity against PBP2' receptor in Staphylococcus aureus.
|
Staphylococcus aureus
|
430.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Synthesis and antibacterial activity of lipophilic carbapenems with anti-MRSA activity
Year : 1996
Volume : 6
Issue : 20
First Page : 2449
Last Page : 2454
Authors : Arnould JC, Illingworth RN, Nichols WW, Geoffrey Wilson R
|
Compound was tested for its binding affinity against PBP2'' receptor in Staphylococcus aureus. Values taken from literature.
|
Staphylococcus aureus
|
220.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Synthesis and antibacterial activity of lipophilic carbapenems with anti-MRSA activity
Year : 1996
Volume : 6
Issue : 20
First Page : 2449
Last Page : 2454
Authors : Arnould JC, Illingworth RN, Nichols WW, Geoffrey Wilson R
|
PBP-2'' affinity was determined by the competition assay with [14C]benzylpenicillin using membrane isolated from MRSA BB6294 strain
|
Staphylococcus aureus
|
125.0
ug.mL-1
|
|
Journal : Bioorg. Med. Chem. Lett.
Title : Novel dithiocarbamate carbapenems1 with anti-MRSA activity
Year : 1997
Volume : 7
Issue : 13
First Page : 1617
Last Page : 1622
Authors : Ohtake N, Imamura H, Kiyonaga H, Jona H, Ogawa M, Okada S, Shimizu A, Moriya M, Sato H, Tominaga Y, Yamada K, Nakano M, Ushijima R, Nakagawa S
|
Inhibitory concentration against purified PBP2x from Streptococcus pneumoniae
|
Streptococcus pneumoniae
|
500.0
nM
|
|
Journal : J. Med. Chem.
Title : Synthesis and structure-activity relationship of (lactamylvinyl)cephalosporins exhibiting activity against staphylococci, pneumococci, and enterococci.
Year : 1996
Volume : 39
Issue : 9
First Page : 1864
Last Page : 1871
Authors : Heinze-Krauss I, Angehrn P, Guerry P, Hebeisen P, Hubschwerlen C, Kompis I, Page MG, Richter HG, Runtz V, Stalder H, Weiss U, Wei CC.
Abstract : The synthesis and structure-activity relationships of a new class of vinylcephalosporins substituted with a lactamyl residue are described. These compounds show excellent activity against enterococci and retain the broad spectrum activity of third-generation cephalosporins such as ceftriaxone.
|
Inhibitory concentration against purified cephalosporin-resistant PBP2x.505 from Streptococcus pneumoniae
|
Streptococcus pneumoniae
|
500.0
nM
|
|
Journal : J. Med. Chem.
Title : Synthesis and structure-activity relationship of (lactamylvinyl)cephalosporins exhibiting activity against staphylococci, pneumococci, and enterococci.
Year : 1996
Volume : 39
Issue : 9
First Page : 1864
Last Page : 1871
Authors : Heinze-Krauss I, Angehrn P, Guerry P, Hebeisen P, Hubschwerlen C, Kompis I, Page MG, Richter HG, Runtz V, Stalder H, Weiss U, Wei CC.
Abstract : The synthesis and structure-activity relationships of a new class of vinylcephalosporins substituted with a lactamyl residue are described. These compounds show excellent activity against enterococci and retain the broad spectrum activity of third-generation cephalosporins such as ceftriaxone.
|
Inhibition of Enterococcus faecium LD-transpeptidase assessed by formation of Ac2-L-Lys-D-[14C]Ala from Ac2-L-Lys-D-Ala and D-[14C]Ala
|
Enterococcus faecium
|
0.077
ug.mL-1
|
|
Journal : J. Biol. Chem.
Title : Unexpected inhibition of peptidoglycan LD-transpeptidase from Enterococcus faecium by the beta-lactam imipenem.
Year : 2007
Volume : 282
Issue : 42
First Page : 30414
Last Page : 30422
Authors : Mainardi JL, Hugonnet JE, Rusconi F, Fourgeaud M, Dubost L, Moumi AN, Delfosse V, Mayer C, Gutmann L, Rice LB, Arthur M.
Abstract : The beta-lactam antibiotics mimic the D-alanyl(4)-D-alanine(5) extremity of peptidoglycan precursors and act as "suicide" substrates of the DD-transpeptidases that catalyze the last cross-linking step of peptidoglycan synthesis. We have previously shown that bypass of the dd-transpeptidases by the LD-transpeptidase of Enterococcus faecium (Ldt(fm)) leads to high level resistance to ampicillin. Ldt(fm) is specific for the L-lysyl(3)-D-alanine(4) bond of peptidoglycan precursors containing a tetrapeptide stem lacking D-alanine(5). This specificity was proposed to account for resistance, because the substrate of Ldt(fm) does not mimic beta-lactams in contrast to the D-alanyl(4)-D-alanine(5) extremity of pentapeptide stems used by the DD-transpeptidases. Here, we unexpectedly show that imipenem, a beta-lactam of the carbapenem class, totally inhibited Ldt(fm) at a low drug concentration that was sufficient to inhibit growth of the bacteria. Peptidoglycan cross-linking was also inhibited, indicating that Ldt(fm) is the in vivo target of imipenem. Stoichiometric and covalent modification of Ldt(fm) by imipenem was detected by mass spectrometry. The modification was mapped into the trypsin fragment of Ldt(fm) containing the catalytic Cys residue, and the Cys to Ala substitution prevented imipenem binding. The mass increment matched the mass of imipenem, indicating that inactivation of Ldt(fm) is likely to involve rupture of the beta-lactam ring and acylation of the catalytic Cys residue. Thus, the spectrum of activity of beta-lactams is not restricted to transpeptidases of the DD-specificity, as previously thought. Combination therapy with imipenem and ampicillin could therefore be active against E. faecium strains having the dual capacity to manufacture peptidoglycan with transpeptidases of the LD- and DD-specificities.
|
Inhibition of Citrobacter freundii PER2 beta lactamase
|
Citrobacter freundii
|
60.0
nM
|
|
Journal : Antimicrob. Agents Chemother.
Title : Biochemical characterization of PER-2 and genetic environment of blaPER-2.
Year : 2007
Volume : 51
Issue : 7
First Page : 2359
Last Page : 2365
Authors : Power P, Di Conza J, Rodríguez MM, Ghiglione B, Ayala JA, Casellas JM, Radice M, Gutkind G.
Abstract : PER-2 was the first detected and the second most prevalent extended-spectrum beta-lactamase in clinical pathogens isolated in Argentina and was also reported only in other South American countries. Citrobacter freundii 33587 was isolated in 1999 in Buenos Aires and was resistant to all tested beta-lactams except cephamycins and carbapenems. The strain produced both plasmid-borne TEM-1 and PER-2 (pI 5.4), which could be transferred by conjugation. By PCR screening, thermal asymmetric interlaced PCR, and DNA sequencing, we detected an ISPa12/IS1387a insertion sequence upstream of bla(PER-2), previously reported as also being associated with bla(PER-1). The presence of similar structures upstream of bla(PER-1) and bla(PER-2) suggests a common origin and mobilization. Compared to bla(PER-1) genes, an additional putative promoter for bla(PER-2) was found. PER-2 kinetic analysis showed its high hydrolysis efficiencies toward both CTX and CAZ (k(cat)/K(m), 0.76 and 0.43 microM(-1).s(-1), respectively).
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 1b
|
Pseudomonas aeruginosa PAO1
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 1a
|
Pseudomonas aeruginosa PAO1
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 6
|
Escherichia coli
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 5
|
Escherichia coli
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 4
|
Escherichia coli
|
0.01
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 3
|
Escherichia coli
|
8.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 2
|
Escherichia coli
|
0.01
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 1b
|
Escherichia coli
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Escherichia coli MC4100 penicillin-binding protein 1a
|
Escherichia coli
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 2
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 3
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 4
|
Pseudomonas aeruginosa PAO1
|
0.01
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of bocillin FL binding to Pseudomonas aeruginosa PAO1 penicillin-binding protein 5/6
|
Pseudomonas aeruginosa PAO1
|
2.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae.
Year : 2007
Volume : 51
Issue : 7
First Page : 2621
Last Page : 2624
Authors : Davies TA, Page MG, Shang W, Andrew T, Kania M, Bush K.
Abstract : Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.
|
Inhibition of Pseudomonas aeruginosa GES-13 beta lactamase
|
Pseudomonas aeruginosa
|
150.0
nM
|
|
Journal : Antimicrob. Agents Chemother.
Title : GES-13, a beta-lactamase variant possessing Lys-104 and Asn-170 in Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 3
First Page : 1331
Last Page : 1333
Authors : Kotsakis SD, Papagiannitsis CC, Tzelepi E, Legakis NJ, Miriagou V, Tzouvelekis LS.
Abstract : GES-13 beta-lactamase, a novel GES variant possessing Lys-104 and Asn-170, was identified in Pseudomonas aeruginosa. bla(GES-13) was the single gene cassette of a class 1 integron probably located in the chromosome. GES-13 efficiently hydrolyzed broad-spectrum cephalosporins and aztreonam. Imipenem was a potent inhibitor of GES-13 but was not hydrolyzed at measurable rates.
|
Inhibition of Bocillin FL binding to PBP1A in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.5
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP1B in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.4
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP2 in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.008
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP3 in Escherichia coli MC4100 membranes
|
Escherichia coli
|
8.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP4 in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.01
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP5 in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.4
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP6 in Escherichia coli MC4100 membranes
|
Escherichia coli
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP1A in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP1B in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
0.2
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP2 in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP3 in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
0.09
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP4 in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
0.008
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP5/6 in Pseudomonas aeruginosa PAO1 membranes
|
Pseudomonas aeruginosa PAO1
|
2.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP1A in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP1B in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP2 in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP3 in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
0.3
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP4 in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
0.008
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of Bocillin FL binding to PBP5/6 in Pseudomonas aeruginosa 27853 membranes
|
Pseudomonas aeruginosa PAO1
|
1.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of doripenem and comparators to penicillin-binding proteins in Escherichia coli and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 4
First Page : 1510
Last Page : 1512
Authors : Davies TA, Shang W, Bush K, Flamm RK.
Abstract : Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.
|
Inhibition of VIM-1 activity in Escherichia coli extracts at 100 uM
|
Escherichia coli
|
95.0
%
|
|
Journal : Antimicrob. Agents Chemother.
Title : Outbreak of Acinetobacter baumannii with chromosomally encoded VIM-1 undetectable by imipenem-EDTA synergy tests.
Year : 2008
Volume : 52
Issue : 5
First Page : 1894
Last Page : 1896
Authors : Loli A, Tzouvelekis LS, Gianneli D, Tzelepi E, Miriagou V.
|
Binding affinity to PBP2a in methicillin-resistant Staphylococcus aureus 123-1 by [14C]benzylpenicillin labelled competitive assay
|
Staphylococcus aureus
|
170.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Potent in vitro activity of tomopenem (CS-023) against methicillin-resistant Staphylococcus aureus and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 8
First Page : 2849
Last Page : 2854
Authors : Koga T, Masuda N, Kakuta M, Namba E, Sugihara C, Fukuoka T.
Abstract : Tomopenem (formerly CS-023) is a novel 1beta-methylcarbapenem with broad-spectrum coverage of gram-positive and gram-negative pathogens. Its antibacterial activity against European clinical isolates of methicillin-resistant Staphylococcus aureus (MRSA) and Pseudomonas aeruginosa was compared with those of imipenem and meropenem. The MICs of tomopenem against MRSA and P. aeruginosa at which 90% of the isolates tested were inhibited were 8 and 4 microg/ml, respectively, and were equal to or more than fourfold lower than those of imipenem and meropenem. The antibacterial activity of tomopenem against MRSA was correlated with a higher affinity for the penicillin-binding protein (PBP) 2a. Its activity against laboratory mutants of P. aeruginosa with (i) overproduction of chromosomally coded AmpC beta-lactamase; (ii) overproduction of the multidrug efflux pumps MexAB-OprM, MexCD-OprJ, and MexEF-OprN; (iii) deficiency in OprD; and (iv) various combinations of AmpC overproduction, MexAB-OprM overproduction, and OprD deficiency were tested. The increases in the MIC of tomopenem against each single mutant compared with that against its parent strain were within a fourfold range. Tomopenem exhibited antibacterial activity against all mutants, with an observed MIC range of 0.5 to 8 microg/ml. These results suggest that the antibacterial activity of tomopenem against the clinical isolates of MRSA and P. aeruginosa should be ascribed to its high affinity for PBP 2a and its activity against the mutants of P. aeruginosa, respectively.
|
Binding affinity to PBP2a in methicillin-resistant Staphylococcus aureus 12386-1 by [14C]benzylpenicillin labelled competitive assay
|
Staphylococcus aureus
|
76.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Potent in vitro activity of tomopenem (CS-023) against methicillin-resistant Staphylococcus aureus and Pseudomonas aeruginosa.
Year : 2008
Volume : 52
Issue : 8
First Page : 2849
Last Page : 2854
Authors : Koga T, Masuda N, Kakuta M, Namba E, Sugihara C, Fukuoka T.
Abstract : Tomopenem (formerly CS-023) is a novel 1beta-methylcarbapenem with broad-spectrum coverage of gram-positive and gram-negative pathogens. Its antibacterial activity against European clinical isolates of methicillin-resistant Staphylococcus aureus (MRSA) and Pseudomonas aeruginosa was compared with those of imipenem and meropenem. The MICs of tomopenem against MRSA and P. aeruginosa at which 90% of the isolates tested were inhibited were 8 and 4 microg/ml, respectively, and were equal to or more than fourfold lower than those of imipenem and meropenem. The antibacterial activity of tomopenem against MRSA was correlated with a higher affinity for the penicillin-binding protein (PBP) 2a. Its activity against laboratory mutants of P. aeruginosa with (i) overproduction of chromosomally coded AmpC beta-lactamase; (ii) overproduction of the multidrug efflux pumps MexAB-OprM, MexCD-OprJ, and MexEF-OprN; (iii) deficiency in OprD; and (iv) various combinations of AmpC overproduction, MexAB-OprM overproduction, and OprD deficiency were tested. The increases in the MIC of tomopenem against each single mutant compared with that against its parent strain were within a fourfold range. Tomopenem exhibited antibacterial activity against all mutants, with an observed MIC range of 0.5 to 8 microg/ml. These results suggest that the antibacterial activity of tomopenem against the clinical isolates of MRSA and P. aeruginosa should be ascribed to its high affinity for PBP 2a and its activity against the mutants of P. aeruginosa, respectively.
|
Antibacterial activity against Staphylococcus aureus ATCC 6538P by microdilution method
|
Staphylococcus aureus
|
0.008
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Antibacterial activity against Escherichia coli NIHJ by microdilution method
|
Escherichia coli
|
0.25
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Antibacterial activity against Pseudomonas aeruginosa ATCC 15692 by microdilution method
|
Pseudomonas aeruginosa
|
1.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP1 in Staphylococcus aureus ATCC 6538P
|
Staphylococcus aureus
|
0.024
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP2 Staphylococcus aureus ATCC 6538P
|
Staphylococcus aureus
|
0.047
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP3 in Staphylococcus aureus ATCC 6538P
|
Staphylococcus aureus
|
0.049
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP4 in Staphylococcus aureus ATCC 6538P
|
Staphylococcus aureus
|
0.0078
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP1A in Escherichia coli NIHJ
|
Escherichia coli
|
0.22
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP1B in Escherichia coli NIHJ
|
Escherichia coli
|
1.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP2 in Escherichia coli NIHJ
|
Escherichia coli
|
0.045
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP3 in Escherichia coli NIHJ
|
Escherichia coli
|
19.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP4 in Escherichia coli NIHJ
|
Escherichia coli
|
0.44
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP5 in Escherichia coli NIHJ
|
Escherichia coli
|
0.34
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP6 Escherichia coli NIHJ
|
Escherichia coli
|
1.0
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP1A in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.057
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP1B in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.078
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP2 in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.066
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP3 in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.089
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP4 in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.0032
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP 5 in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.19
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of [14C]benzylpenicillin from PBP 6 in Pseudomonas aeruginosa ATCC 15692
|
Pseudomonas aeruginosa
|
0.19
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of Tomopenem (CS-023) for penicillin-binding proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa.
Year : 2009
Volume : 53
Issue : 3
First Page : 1238
Last Page : 1241
Authors : Koga T, Sugihara C, Kakuta M, Masuda N, Namba E, Fukuoka T.
Abstract : Tomopenem (formerly CS-023), a novel 1beta-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP1A
|
Streptococcus pneumoniae
|
0.441
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP1A
|
Streptococcus pneumoniae
|
0.62
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP1A
|
Streptococcus pneumoniae
|
0.042
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP1A
|
Streptococcus pneumoniae
|
0.251
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP1A
|
Streptococcus pneumoniae
|
0.182
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP1A
|
Streptococcus pneumoniae
|
0.289
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP1A
|
Streptococcus pneumoniae
|
0.026
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP1A
|
Streptococcus pneumoniae
|
0.09
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP1A
|
Streptococcus pneumoniae
|
0.052
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP1B
|
Streptococcus pneumoniae
|
0.71
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP1B
|
Streptococcus pneumoniae
|
0.316
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP1B
|
Streptococcus pneumoniae
|
0.023
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP1B
|
Streptococcus pneumoniae
|
0.182
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP1B
|
Streptococcus pneumoniae
|
0.108
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP1B
|
Streptococcus pneumoniae
|
0.077
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP1B
|
Streptococcus pneumoniae
|
0.009
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP1B
|
Streptococcus pneumoniae
|
0.031
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP1B
|
Streptococcus pneumoniae
|
0.106
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2X
|
Streptococcus pneumoniae
|
2.048
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2X
|
Streptococcus pneumoniae
|
0.429
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2X
|
Streptococcus pneumoniae
|
0.018
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2X
|
Streptococcus pneumoniae
|
0.039
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP2X
|
Streptococcus pneumoniae
|
0.19
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2X
|
Streptococcus pneumoniae
|
0.592
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2X
|
Streptococcus pneumoniae
|
0.1
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2X
|
Streptococcus pneumoniae
|
0.059
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP2X
|
Streptococcus pneumoniae
|
0.179
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2A
|
Streptococcus pneumoniae
|
0.352
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2A
|
Streptococcus pneumoniae
|
0.337
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2A
|
Streptococcus pneumoniae
|
0.059
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2A
|
Streptococcus pneumoniae
|
0.115
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2A
|
Streptococcus pneumoniae
|
0.233
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2A
|
Streptococcus pneumoniae
|
0.054
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2A
|
Streptococcus pneumoniae
|
0.054
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP2B
|
Streptococcus pneumoniae
|
0.132
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP2B
|
Streptococcus pneumoniae
|
0.866
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP2B
|
Streptococcus pneumoniae
|
0.062
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP2B
|
Streptococcus pneumoniae
|
0.396
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP2B
|
Streptococcus pneumoniae
|
0.066
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP2B
|
Streptococcus pneumoniae
|
0.651
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP2B
|
Streptococcus pneumoniae
|
0.046
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP2B
|
Streptococcus pneumoniae
|
0.071
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP2B
|
Streptococcus pneumoniae
|
0.046
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 24 PBP3
|
Streptococcus pneumoniae
|
0.2
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3413 PBP3
|
Streptococcus pneumoniae
|
0.195
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 2527 PBP3
|
Streptococcus pneumoniae
|
0.034
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3676 PBP3
|
Streptococcus pneumoniae
|
0.188
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3243 PBP3
|
Streptococcus pneumoniae
|
0.095
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3665 PBP3
|
Streptococcus pneumoniae
|
0.171
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 3009 PBP3
|
Streptococcus pneumoniae
|
0.039
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1076 PBP3
|
Streptococcus pneumoniae
|
0.032
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Displacement of Biocillin FL from Streptococcus pneumoniae 1077 PBP3
|
Streptococcus pneumoniae
|
0.219
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Binding of faropenem and other beta-lactam agents to penicillin-binding proteins of pneumococci with various beta-lactam susceptibilities.
Year : 2009
Volume : 53
Issue : 5
First Page : 2176
Last Page : 2180
Authors : Kosowska-Shick K, McGhee P, Appelbaum PC.
Abstract : Faropenem demonstrated low MICs (< or = 1 microg/ml) for all penicillin-susceptible and nonsusceptible pneumococci and exhibited very strong abilities to bind to Streptococcus pneumoniae penicillin-binding proteins (PBPs), except for PBP2X. The lower faropenem affinity for PBP2X did not affect MICs for any strains tested, and only imipenem had lower MICs, with much lower binding affinities for all PBPs tested, than faropenem.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP1b by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.13
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP1c by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.08
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP2 by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.08
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP3 by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.12
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP4 by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.02
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of Pseudomonas aeruginosa PAO1 PBP5/6 by SDS-PAGE
|
Pseudomonas aeruginosa PAO1
|
0.2
ug.mL-1
|
|
Journal : Antimicrob. Agents Chemother.
Title : Affinity of the new cephalosporin CXA-101 to penicillin-binding proteins of Pseudomonas aeruginosa.
Year : 2010
Volume : 54
Issue : 9
First Page : 3933
Last Page : 3937
Authors : Moyá B, Zamorano L, Juan C, Ge Y, Oliver A.
Abstract : CXA-101, previously designated FR264205, is a new antipseudomonal cephalosporin. The objective of this study was to determine the penicillin-binding protein (PBP) inhibition profile of CXA-101 compared to that of ceftazidime (PBP3 inhibitor) and imipenem (PBP2 inhibitor). Killing kinetics, the induction of AmpC expression, and associated changes on cell morphology were also investigated. The MICs for CXA-101, ceftazidime, and imipenem were 0.5, 1, and 1 microg/ml, respectively. Killing curves revealed that CXA-101 shows a concentration-independent bactericidal activity, with concentrations of 1x the MIC (0.5 microg/ml) producing a > 3-log reduction in bacterial load after 8 h of incubation. Live-dead staining showed that concentrations of CXA-101 as low as 0.5x the MIC stopped bacterial septation and induced an intense filamentation, which is consistent with the documented high affinity of PBP3. CXA-101 was found to be a potent PBP3 inhibitor and showed affinities > or = 2-fold higher than those of ceftazidime for all of the essential PBPs (1b, 1c, 2, and 3). Compared to imipenem, in addition to the obvious inverse PBP2/PBP3 affinities, CXA-101 showed a significantly higher affinity for PBP1b but a lower affinity for PBP1c. Furthermore, CXA-101, like ceftazidime and in contrast to imipenem, was found to be a very weak inducer of AmpC expression, consistent with the low PBP4 affinity documented.
|
Inhibition of recombinant human GABA A alpha2beta2gamma2 receptor expressed in CHO-K1 cells at 300 uM incubated at room temperature for 15 mins before the GABA addition fluorescence spectrometry
|
Homo sapiens
|
15.0
%
|
|
Journal : Bioorg Med Chem Lett
Title : Optimization of novel monobactams with activity against carbapenem-resistant Enterobacteriaceae - Identification of LYS228.
Year : 2018
Volume : 28
Issue : 4
First Page : 748
Last Page : 755
Authors : Reck F, Bermingham A, Blais J, Capka V, Cariaga T, Casarez A, Colvin R, Dean CR, Fekete A, Gong W, Growcott E, Guo H, Jones AK, Li C, Li F, Lin X, Lindvall M, Lopez S, McKenney D, Metzger L, Moser HE, Prathapam R, Rasper D, Rudewicz P, Sethuraman V, Shen X, Shaul J, Simmons RL, Tashiro K, Tang D, Tjandra M, Turner N, Uehara T, Vitt C, Whitebread S, Yifru A, Zang X, Zhu Q.
Abstract : Metallo-β-lactamases (MBLs), such as New Delhi metallo-β-lactamase (NDM-1) have spread world-wide and present a serious threat. Expression of MBLs confers resistance in Gram-negative bacteria to all classes of β-lactam antibiotics, with the exception of monobactams, which are intrinsically stable to MBLs. However, existing first generation monobactam drugs like aztreonam have limited clinical utility against MBL-expressing strains because they are impacted by serine β-lactamases (SBLs), which are often co-expressed in clinical isolates. Here, we optimized novel monobactams for stability against SBLs, which led to the identification of LYS228 (compound 31). LYS228 is potent in the presence of all classes of β-lactamases and shows potent activity against carbapenem-resistant isolates of Enterobacteriaceae (CRE).
|
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of Caco-2 cells at 10 uM after 48 hours by high content imaging
|
Homo sapiens
|
0.03
%
|
|
Title : Identification of inhibitors of SARS-CoV-2 in-vitro cellular toxicity in human (Caco-2) cells using a large scale drug repurposing collection
Year : 2020
Authors : Bernhard Ellinger, Denisa Bojkova, Andrea Zaliani, Jindrich Cinatl, Carsten Claussen, Sandra Westhaus, Jeanette Reinshagen, Maria Kuzikov, Markus Wolf, Gerd Geisslinger, Philip Gribbon, Sandra Ciesek
Abstract : To identify possible candidates for progression towards clinical studies against SARS-CoV-2, we screened a well-defined collection of 5632 compounds including 3488 compounds which have undergone clinical investigations (marketed drugs, phases 1 -3, and withdrawn) across 600 indications. Compounds were screened for their inhibition of viral induced cytotoxicity using the human epithelial colorectal adenocarcinoma cell line Caco-2 and a SARS-CoV-2 isolate. The primary screen of 5632 compounds gave 271 hits. A total of 64 compounds with IC50 <20 µM were identified, including 19 compounds with IC50 < 1 µM. Of this confirmed hit population, 90% have not yet been previously reported as active against SARS-CoV-2 in-vitro cell assays. Some 37 of the actives are launched drugs, 19 are in phases 1-3 and 10 pre-clinical. Several inhibitors were associated with modulation of host pathways including kinase signaling P53 activation, ubiquitin pathways and PDE activity modulation, with long chain acyl transferases were effective viral inhibitors.
|
SARS-CoV-2 3CL-Pro protease inhibition percentage at 20µM by FRET kind of response from peptide substrate
|
Severe acute respiratory syndrome coronavirus 2
|
10.2
%
|
|
Title : Identification of inhibitors of SARS-Cov2 M-Pro enzymatic activity using a small molecule repurposing screen
Year : 2020
Authors : Maria Kuzikov, Elisa Costanzi, Jeanette Reinshagen, Francesca Esposito, Laura Vangeel, Markus Wolf, Bernhard Ellinger, Carsten Claussen, Gerd Geisslinger, Angela Corona, Daniela Iaconis, Carmine Talarico, Candida Manelfi, Rolando Cannalire, Giulia Rossetti, Jonas Gossen, Simone Albani, Francesco Musiani, Katja Herzog, Yang Ye, Barbara Giabbai, Nicola Demitri, Dirk Jochmans, Steven De Jonghe, Jasper Rymenants, Vincenzo Summa, Enzo Tramontano, Andrea R. Beccari, Pieter Leyssen, Paola Storici, Johan Neyts, Philip Gribbon, and Andrea Zaliani
Abstract : Compound repurposing is an important strategy being pursued in the identification of effective treatment against the SARS-CoV-2 infection and COVID-19 disease. In this regard, SARS-CoV-2 main protease (M-Pro), also termed 3CL-Pro, is an attractive drug target as it plays a central role in viral replication by processing the viral polyprotein into 11 non-structural proteins. We report the results of a screening campaign involving ca 8.7 K compounds containing marketed drugs, clinical and preclinical candidates, and chemicals regarded as safe in humans. We confirmed previously reported inhibitors of 3CL-Pro, but we have also identified 68 compounds with IC50 lower than 1 uM and 127 compounds with IC50 lower than 5 uM. Profiling showed 67% of confirmed hits were selective (> 5 fold) against other Cys- and Ser- proteases (Chymotrypsin and Cathepsin-L) and MERS 3CL-Pro. Selected compounds were also analysed in their binding characteristics.
|
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging
|
Chlorocebus sabaeus
|
-0.05
%
|
|
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging
|
Chlorocebus sabaeus
|
-0.05
%
|
|
Title : Cytopathic SARS-Cov2 screening on VERO-E6 cells in a large repurposing effort
Year : 2020
Authors : Andrea Zaliani, Laura Vangeel, Jeanette Reinshagen, Daniela Iaconis, Maria Kuzikov, Oliver Keminer, Markus Wolf, Bernhard Ellinger, Francesca Esposito, Angela Corona, Enzo Tramontano, Candida Manelfi, Katja Herzog, Dirk Jochmans, Steven De Jonghe, Winston Chiu, Thibault Francken, Joost Schepers, Caroline Collard, Kayvan Abbasi, Carsten Claussen , Vincenzo Summa, Andrea R. Beccari, Johan Neyts, Philip Gribbon and Pieter Leyssen
Abstract : Worldwide, there are intensive efforts to identify repurposed drugs as potential therapies against SARS-CoV-2 infection and the associated COVID-19 disease. To date, the anti-inflammatory drug dexamethasone and (to a lesser extent) the RNA-polymerase inhibitor remdesivir have been shown to be effective in reducing mortality and patient time to recovery, respectively, in patients. Here, we report the results of a phenotypic screening campaign within an EU-funded project (H2020-EXSCALATE4COV) aimed at extending the repertoire of anti-COVID therapeutics through repurposing of available compounds and highlighting compounds with new mechanisms of action against viral infection. We screened 8702 molecules from different repurposing libraries, to reveal 110 compounds with an anti-cytopathic IC50 < 20 µM. From this group, 18 with a safety index greater than 2 are also marketed drugs, making them suitable for further study as potential therapies against COVID-19. Our result supports the idea that a systematic approach to repurposing is a valid strategy to accelerate the necessary drug discovery process.
