POINT MUTATIONS IN STAPHYLOCOCCUS-AUREUS PBP-2 GENE AFFECT PENICILLIN-BINDING KINETICS AND ARE ASSOCIATED WITH RESISTANCE

被引：72

作者：

HACKBARTH, CJ ^{[1
]}

KOCAGOZ, T ^{[1
]}

KOCAGOZ, S ^{[1
]}

CHAMBERS, HF ^{[1
]}

机构：

[1] SAN FRANCISCO GEN HOSP, DIV INFECT DIS, SAN FRANCISCO, CA 94110 USA

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 1995年 / 39卷 / 01期

关键词：

D O I：

10.1128/AAC.39.1.103

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

In Staphylococcus aureus, penicillin-binding protein 2 (PBP 2) has been implicated in non-PBP 2a-mediated methicillin resistance. The PBP 2 gene (bpbB) was cloned from an expression library of a methicillin susceptible strain of S. aureus (209P), and its entire sequence was compared with that of the pbpB gene from strains BB255, BB255R, and CDC6. Point mutations that resulted in amino acid substitutions near the conserved penicillin-binding motifs were detected in BB255R and CDC6, two low-level methicillin-resistant strains. Penicillin binding to PBP 2 in both BB255R and CDC6 is altered, and kinetic analysis indicated that altered binding of PBP 2 by penicillin was due to both lower binding affinity and more rapid release of bound drug. These structural and biochemical changes may contribute to the strains' resistance to beta-lactam antibiotics.

引用

页码：103 / 106

页数：4

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