Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus. Academic Article uri icon

Overview

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.

publication date

  • May 1, 1984

Research

keywords

  • Bacterial Proteins
  • Carboxypeptidases
  • Carrier Proteins
  • Hexosyltransferases
  • Methicillin
  • Muramoylpentapeptide Carboxypeptidase
  • Peptidyl Transferases
  • Staphylococcus aureus

Identity

PubMed Central ID

  • PMC215458

Scopus Document Identifier

  • 0021361020

Digital Object Identifier (DOI)

  • 10.1128/jb.158.2.513-516.1984

PubMed ID

  • 6563036

Additional Document Info

volume

  • 158

issue

  • 2