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膜融合蛋白 AdeT1 对大肠杆菌抗菌耐药性的影响。

Effect of membrane fusion protein AdeT1 on the antimicrobial resistance of Escherichia coli.

机构信息

School of Chemistry, Cardiff University, Cardiff, UK.

Graduate Institute of Biomedical Sciences, China Medical University, Taichung, Taiwan.

出版信息

Sci Rep. 2020 Nov 24;10(1):20464. doi: 10.1038/s41598-020-77339-w.

DOI:10.1038/s41598-020-77339-w
PMID:33235243
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7687900/
Abstract

Acinetobacter baumannii is a prevalent pathogen that can rapidly acquire resistance to antibiotics. Indeed, multidrug-resistant A. baumannii is a major cause of hospital-acquired infections and has been recognised by the World Health Organization as one of the most threatening bacteria to our society. Resistance-nodulation-division (RND) type multidrug efflux pumps have been demonstrated to convey antibiotic resistance to a wide range of pathogens and are the primary resistance mechanism employed by A. baumannii. A component of an RND pump in A. baumannii, AdeT1, was previously demonstrated to enhance the antimicrobial resistance of Escherichia coli. Here, we report the results of experiments which demonstrate that wild-type AdeT1 does not confer antimicrobial resistance in E. coli, highlighting the importance of verifying protein production when determining minimum inhibitory concentrations (MICs) especially by broth dilution. Nevertheless, using an agar-based MIC assay, we found that propionylation of Lys280 on AdeT1 renders E. coli cells more resistant to erythromycin.

摘要

鲍曼不动杆菌是一种流行的病原体，能够迅速获得抗生素耐药性。事实上，耐多药鲍曼不动杆菌是医院获得性感染的主要原因，世界卫生组织已将其列为对我们社会最具威胁的细菌之一。已证实，耐药-结节-分裂（RND）型多药外排泵可将抗生素耐药性传递给广泛的病原体，是鲍曼不动杆菌采用的主要耐药机制。先前已经证明，鲍曼不动杆菌 RND 泵的一个组成部分 AdeT1 可增强大肠杆菌的抗菌药物耐药性。在这里，我们报告的实验结果表明野生型 AdeT1 不会赋予大肠杆菌抗菌药物耐药性，这突出表明在确定最低抑菌浓度（MIC）时，特别是通过肉汤稀释法，验证蛋白质表达的重要性。尽管如此，我们发现使用基于琼脂的 MIC 测定法，AdeT1 上赖氨酸 280 的丙酰化作用使大肠杆菌细胞对红霉素更具耐药性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/b54fb16b745c/41598_2020_77339_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/769086255562/41598_2020_77339_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/c88d96ce3121/41598_2020_77339_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/1656fad21c81/41598_2020_77339_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/88225d9732f7/41598_2020_77339_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/aeccd1a25239/41598_2020_77339_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/b0dc85a2b72b/41598_2020_77339_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/05beb40f2272/41598_2020_77339_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/27966e0f4c9b/41598_2020_77339_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/b54fb16b745c/41598_2020_77339_Fig9_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/769086255562/41598_2020_77339_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/c88d96ce3121/41598_2020_77339_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/1656fad21c81/41598_2020_77339_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/88225d9732f7/41598_2020_77339_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/aeccd1a25239/41598_2020_77339_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/b0dc85a2b72b/41598_2020_77339_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/05beb40f2272/41598_2020_77339_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/27966e0f4c9b/41598_2020_77339_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d054/7687900/b54fb16b745c/41598_2020_77339_Fig9_HTML.jpg

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