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Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus

Journal of Bacteriology · 1984 · Vol. 158(2) · pp. 513–516

Abstract

Methicillin resistance in Staphylococcus aureus has been associated with alterations in the penicillin-binding proteins (PBPs). An intriguing property of all methicillin-resistant staphylococci is the dependence of resistance on the pH value of the growth medium. Growth of such bacteria at pH 5.2 completely suppressed the expression of methicillin resistance. We have examined the PBP patterns of methicillin-resistant staphylococci grown at pH 7.0. We detected a high-molecular-weight PBP (PBP-2a; approximate size, 78,000 daltons) that was only present in the resistant bacteria but not in the isogenic sensitive strain. In cultures grown at pH 5.2, the extra PBP was not detectable.

Antimicrobial Resistance in StaphylococcusBiochemical and Structural CharacterizationToxin Mechanisms and ImmunotoxinsPenicillin binding proteinsStaphylococcus aureusMicrobiologyBiologyPenicillinBacteriaPenicillin resistanceMicrococcaceaeStaphylococcusAntibiotics

MeSH terms

Bacterial ProteinsMuramoylpentapeptide CarboxypeptidaseCarboxypeptidasesCarrier ProteinsHexosyltransferasesHydrogen-Ion ConcentrationMethicillinMolecular WeightPenicillin ResistancePeptidyl TransferasesStaphylococcus aureusPenicillin-Binding Proteins
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