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青霉素结合蛋白在阴沟肠杆菌AmpC β-内酰胺酶表达起始中的作用

Role of penicillin-binding proteins in the initiation of the AmpC beta-lactamase expression in Enterobacter cloacae.

作者信息

Pfeifle D, Janas E, Wiedemann B

机构信息

Pharmazeutische Mikrobiologie, University of Bonn, 53115 Bonn, Germany.

出版信息

Antimicrob Agents Chemother. 2000 Jan;44(1):169-72. doi: 10.1128/AAC.44.1.169-172.2000.

DOI:10.1128/AAC.44.1.169-172.2000
PMID:10602741
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC89646/
Abstract

Penicillin-binding proteins (PBPs) are involved in the regulation of beta-lactamase expression by determining the level of anhydromuramylpeptides in the periplasmatic space. It was hypothesized that one or more PBPs act as a sensor in the beta-lactamase induction pathway. We have performed induction studies with Escherichia coli mutants lacking one to four PBPs with DD-carboxypeptidase activity. Therefore, we conclude that a strong beta-lactamase inducer must inhibit all DD-carboxypeptidases as well as the essential PBPs 1a, 1b, and/or 2.

摘要

青霉素结合蛋白（PBPs）通过确定周质空间中脱水 Muramyl 肽的水平参与β-内酰胺酶表达的调节。据推测，一种或多种 PBPs 在β-内酰胺酶诱导途径中充当传感器。我们对缺乏一至四种具有 DD-羧肽酶活性的 PBPs 的大肠杆菌突变体进行了诱导研究。因此，我们得出结论，一种强β-内酰胺酶诱导剂必须抑制所有 DD-羧肽酶以及必需的 PBPs 1a、1b 和/或 2。

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