MECHANISMS OF RESISTANCE TO BETA-LACTAM ANTIBIOTICS IN ACINETOBACTER-CALCOACETICUS

被引：40

作者：

OBARA, M ^{[1
]}

NAKAE, T ^{[1
]}

机构：

[1] TOKAI UNIV, SCH MED, DEPT CELLULAR INFORMAT SCI, ISEHARA, KANAGAWA 25911, JAPAN

来源：

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY | 1991年 / 28卷 / 06期

关键词：

D O I：

10.1093/jac/28.6.791

中图分类号：

R51 [传染病];

学科分类号：

100401 ;

摘要：

Examination of 12 strains of Acinetobacter calcoaceticus revealed that the strains expressed different constitutive levels of β-lactamase. Mutants resistant to cefoxitin, cefoperazone or ceftazidime were selected from a strain producing a low level of β-lactamase. All the mutants showed no change in expression of β-lactamase, but produced penicillin-binding proteins with altered expression and/or affinity for β-lactamase. In addition, the outer membrane of the mutants showed decreased permeability (40-80% that of the parent strain) towards small hydrophilk solutes, together with diminished production of a 46-5 kDa porin protein. It was concluded that the enhanced resistance to β-lactamase in the A. calcoaceticus mutants was the result of interplay between the altered penicillin binding proteins and the reduced outer membrane permeability. © 1991 by The British Society for Antimicrobial Chemotherapy.

引用

页码：791 / 800

页数：10

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