Methicillin‐resistant Staphylococcus aureus (MRSA) tolerates β‐lactam antibiotics by carrying out cell wall synthesis with the transpeptidase Penicillin‐binding protein 2a (PBP2a), which

Penicillin Binding Protein 2a Staphylococcus. H. Humphreys, in Medical Microbiology (Eighteenth Edition), 2012 MRSA produces a penicillin binding Immunological Methods in Microbiology. Tatsuya Tominaga, Masaharu Ishii, in Methods in Microbiology, 2020 The emergence β-Lactam antibiotics. Karen

lococcus aureus contain an extra penicillin binding protein (PBP) 2A in addition to four PBPs present in all staphylococcal strains. This extra PBP is thought to be a transpeptidase essential for the continued cell wall synthesis and growth in the presence of &lactam antibiotics. As an approach of testing this hypothesis Resistance is associated with production of a penicillin-binding protein (PBP), PBP 2a, with low affinity for binding beta-lactam antibiotics. Therefore, the effects of NaCl and nafcillin on amounts of PBP 2a produced and its binding affinity were examined and correlated with expression of resistance. The gene product, PBP 2a (also termed PBP 2′), is an inducible 76-kDa penicillin-binding protein (PBP). PBP 2a has low affinity for binding β-lactam antibiotics and apparently can substitute for the essential functions of high-affinity PBPs at otherwise lethal concentrations of antibiotic.

The gene product, PBP 2a (also termed PBP 2′), is an inducible 76-kDa penicillin-binding protein (PBP). PBP 2a has low affinity for binding β-lactam antibiotics and apparently can substitute for the essential functions of high-affinity PBPs at otherwise lethal concentrations of antibiotic. LifeSpan BioSciences currently sells 12 antibodies , 1 protein specific for Penicillin Binding Protein 2a. Penicillin binding protein 2a imparts to the human pathogen Staphylococcus aureus resistance to β-lactam antibiotics. Our structural characterization of the allosteric basis governing its resistance mechanism identifies a basis for the design of new antibacterials that can both activate and inhibit this key resistance enzyme.

Status. Unreviewed-Annotation score: -Protein inferred from homology i. Function i GO - Molecular function i.

mecA1 - Penicillin binding protein 2a - Staphylococcus pseudintermedius - mecA1 gene & protein UniProtKB - B5M0C8 (B5M0C8_STAPS)

Bacillus subtilis (strain 168) Status. Reviewed-Annotation score: -Experimental evidence at protein level i. Function i.

The gene encodes the protein PBP2A (Penicillin binding protein 2A). PBP2A has a low affinity for beta-lactam antibiotics such as methicillin and penicillin.

PBP2a stands for Penicillin Binding Protein 2a.

A Scanning electron microscopy (SEM) photograph of Haemophilus av J Larsson · Citerat av 2 — coelicolor sporulation protein WhiH is an autoregulatory transcription 2A and B). whiA and close to a gene coding for a penicillin- binding protein (PBP) with. av C Kellerman · 2019 — Methicillin resistent Staphylococcus aureus.
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Toney JH(1), Hammond GG, Leiting B, Pryor KD, Wu JK, Cuca GC, Pompliano DL. Author information: (1)Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065-0900, USA. jeff_toney@merck.com Bacterial proteins that share the property of binding irreversibly to PENICILLINS and other ANTIBACTERIAL AGENTS derived from LACTAMS. The penicillin-binding proteins are primarily enzymes involved in CELL WALL biosynthesis including MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE ; PEPTIDE SYNTHASES ; TRANSPEPTIDASES ; and HEXOSYLTRANSFERASES .

Because of its low affinity for beta-lactams, PBP2a provides transpeptidase activity to allow cell wall synthesis at beta-lactam concentrations that inhibit the beta-lactam-sensitive PBPs normally produced by S. aureus.
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In contrast, the TP/PBP module has been successfully targeted by β-lactam How allosteric control of Staphylococcus aureus penicillin binding protein 2a