CHARACTERIZATION OF A 38-KDA PENICILLIN-BINDING PROTEIN AND ITS POSSIBLE INVOLVEMENT IN MAINTAINING STATIONARY-PHASE CELLS OF SHIGELLA-DYSENTERIAE

被引：4

作者：

MAHAPATRA, S

BASU, J

VANBEEUMEN, J

KUNDU, M

机构：

[1] BOSE INST, DEPT CHEM, CALCUTTA 700009, W BENGAL, INDIA

[2] RIJKSUNIV GHENT, MICROBIOL LAB, B-9000 GHENT, BELGIUM

来源：

MICROBIOLOGY-SGM | 1994年 / 140卷

关键词：

PENICILLIN-BINDING PROTEIN; SHIGELLA DYSENTERIAE; BETA-LACTAM ANTIBIOTIC;

D O I：

10.1099/13500872-140-11-3177

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

This paper reports the first attempt to characterize the penicillin-binding proteins (PBPs) of Shigella dysenteriae, an important human pathogen. The PBP pattern of the membranes of S. dysenteriae closely resembles that of Escherichia coli membranes. A 38 kDa PBP which is an important target for the penem SCH34343, the cephamycin cefoxitin and the oxacephem moxalactam, has been purified. This PBP is immunologically related to a PBP of similar molecular mass in E. coli and is present at high levels in stationary-phase cells of S. dysenteriae.

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页码：3177 / 3182

页数：6

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