Crystal Structure of Penicillin-Binding Protein 3 (PBP3) from Escherichia coli [PDF]
PLoS ONE, 2014 In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic
Eric Sauvage +2 more
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Potential role of avibactam in restoring susceptibility in Escherichia coli with two copies of blaKPC-3 and PBP3 mutations [PDF]
Scientific ReportsThe emergence of carbapenemase-producing Enterobacterales represents a significant clinical challenge. Resistance mechanisms involve carbapenemase production, porin and efflux pump alterations, penicillin-binding protein (PBP) modifications, and biofilm ...
Valeria Fox +2 more
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Discovery and chemical optimisation of a potent, Bi-cyclic antimicrobial inhibitor of Escherichia coli PBP3 [PDF]
Communications BiologyPenicillin binding proteins (PBPs) are well validated antimicrobial targets, but the prevalence of β-lactamase driven resistance and, more rarely, target-based mutations, necessitates new classes of PBP-targeting drugs. Here we describe the discovery and
Catherine E Rowland, Hector Newman
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Interaction between FtsW and penicillin-binding protein 3 (PBP3) directs PBP3 to mid-cell, controls cell septation and mediates the formation of a trimeric complex involving FtsZ, FtsW and PBP3 in mycobacteria [PDF]
Molecular Microbiology, 2006 SummaryIn bacteria, biogenesis of cell wall at the division site requires penicillin‐binding protein 3 (PBP3) (or FtsI). Using pull‐down, bacterial two‐hybrid, and peptide‐based interaction assays, we provide evidence that FtsW of Mycobacterium tuberculosis (FtsWMTB) interacts with PBP3 through two extracytoplasmic loops.
Pratik Datta +2 more
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Stationary phase persister formation in Escherichia coli can be suppressed by piperacillin and PBP3 inhibition [PDF]
BMC Microbiology, 2019 Background Persisters are rare phenotypic variants within a bacterial population that are capable of tolerating lethal antibiotic concentrations. Passage through stationary phase is associated with the formation of persisters (type I), and a major ...
Sandra Aedo +2 more
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Discovery of Pyrrolidine-2,3-diones as Novel Inhibitors of P. aeruginosa PBP3 [PDF]
Antibiotics, 2021 The alarming threat of the spread of multidrug resistant bacteria currently leaves clinicians with very limited options to combat infections, especially those from Gram-negative bacteria.
Arancha López-Pérez +9 more
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A novel PBP3 substitution in Haemophilus influenzae confers reduced aminopenicillin susceptibility [PDF]
BMC Microbiology, 2018 Background Identification and characterization of non-typeable Haemophilus influenzae (NTHi) with reduced susceptibility to β-lactam antibiotics due to mutations in penicillin binding protein 3 (PBP3) is a clinical challenge. We analyzed a blood isolate,
John Thegerström +4 more
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International Journal of Medical MicrobiologyBackground: Aminopenicillins are recommended agents for non-invasive Haemophilus influenzae infections. One of the mechanisms of resistance to β-lactams is the alteration of the transpeptidase region of penicillin binding protein 3 (PBP3) which is caused
Vladislav Jakubu +2 more
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Influence of the α-Methoxy Group on the Reaction of Temocillin with Pseudomonas aeruginosa PBP3 and CTX-M-14 β-Lactamase [PDF]
Antimicrobial Agents and Chemotherapy, 2019 The prevalence of multidrug-resistant Pseudomonas aeruginosa has led to the reexamination of older “forgotten” drugs, such as temocillin, for their ability to combat resistant microbes. Temocillin is the 6-α-methoxy analogue of ticarcillin, a carboxypenicillin with well-characterized antipseudomonal properties.
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PLoS ONEMultidrug resistance in the Gram-negative bacterial pathogen Acinetobacter baumannii is a global public health threat, highlighting a critical need for drug development.
Eric J. Bryan +6 more
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