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Sensor histidine kinase is a beta-lactam receptor and induces resistance to beta-lactam antibiotics

文献类型： 外文期刊

作者： Li, Lu 1 ; Wang, Qiyao 2 ; Zhang, Hui 1 ; Yang, Minjun 4 ; Khan, Mazhar I. 1 ; Zhou, Xiaohui 1 ;

作者机构： 1.Univ Connecticut, Dept Pathobiol & Vet Sci, Storrs, CT 06269 USA

2.E China Univ Sci & Technol, Sch Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

3.Jiangsu Acad Agr Sci, Nanjing 210014, Jiangsu, Peoples R China

4.Chinese Natl Human Genome Ctr Shanghai, Key Lab Hlth & Dis Genom, Shanghai Minist Sci & Technol MOST, Shanghai 201203, Peoples R China

关键词： Vibrio;histidine kinase;beta-lactam receptor;beta-lactamase

期刊名称：PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA （ 影响因子：11.205； 五年影响因子：12.291 ）

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收录情况： SCI

摘要： beta-Lactams disrupt bacterial cell wall synthesis, and these agents are the most widely used antibiotics. One of the principle mechanisms by which bacteria resist the action of beta-lactams is by producing beta-lactamases, enzymes that degrade beta-lactams. In Gram-negative bacteria, production of beta-lactamases is often induced in response to the antibiotic-associated damage to the cell wall. Here, we have identified a previously unidentified mechanism that governs beta-lactamase production. In the Gram-negative enteric pathogen Vibrio parahaemolyticus, we found a histidine kinase/response regulator pair (VbrK/VbrR) that controls expression of a beta-lactamase. Mutants lacking either VbrK or VbrR do not produce the beta-lactamase and are no longer resistant to beta-lactam antibiotics. Notably, VbrK autophosphorylation is activated by beta-lactam antibiotics, but not by other lactams. However, single amino acid substitutions in the putative periplasmic binding pocket of VbrK leads its phosphorylation in response to both beta-lactam and other lactams, suggesting that this kinase is a beta-lactam receptor that can directly detect beta-lactam antibiotics instead of detecting the damage to cell wall resulting from beta-lactams. In strong support of this idea, we found that purified periplasmic sensor domain of VbrK binds penicillin, and that such binding is critical for VbrK autophosphorylation and beta-lactamase production. Direct recognition of beta-lactam antibiotics by a histidine kinase receptor may represent an evolutionarily favorable mechanism to defend against beta-lactam antibiotics.

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