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耐甲氧西林金黄色葡萄球菌和耐甲氧西林金黄色葡萄球菌对牛髓源抗菌肽(BMAP-28)的敏感性差异。

Susceptibility difference between methicillin-susceptible and methicillin-resistant Staphylococcus aureus to a bovine myeloid antimicrobial peptide (BMAP-28).

机构信息

Laboratory of Animal Microbiology, Tohoku University, Sendai, Japan.

出版信息

Anim Sci J. 2014 Feb;85(2):174-9. doi: 10.1111/asj.12098. Epub 2013 Aug 1.

DOI:10.1111/asj.12098
PMID:23905845
Abstract

A bovine myeloid antimicrobial peptide antimicrobial peptide (BMAP-28) is a member of the cathelicidin family and acts as a component of innate immunity. There are few reports of susceptibility difference of methicillin-resistant Staphylococcus aureus (MRSA) and susceptible strains (MSSA) against BMAP-28. This study aims to clarify how a few amino acid substitutions of BMAP-28 are related to its antimicrobial activity using four analog peptides of BMAP-28. We also compared cellular fatty acid components of MSSA and MRSA using gas chromatography. We found that a few amino acid substitutions of BMAP-28 do not change antimicrobial activity. It was also revealed that the percentage of cis-11-eicosenoic acid in total detected fatty acids of MRSA was significantly higher than that of MSSA. In addition, the percentage of palmitic acid in total detected fatty acids of MRSA tended to be lower than that of MSSA. Our results will provide new information to deal with the question of differences in bacterial susceptibility against BMAP-28.

摘要

一种牛源抗菌肽(BMAP-28)是抗菌肽家族的成员,作为先天免疫的组成部分。关于耐甲氧西林金黄色葡萄球菌(MRSA)和敏感株(MSSA)对 BMAP-28 的敏感性差异的报道较少。本研究旨在使用 BMAP-28 的四个类似肽阐明 BMAP-28 的几个氨基酸取代与抗菌活性之间的关系。我们还使用气相色谱法比较了 MSSA 和 MRSA 的细胞脂肪酸成分。我们发现 BMAP-28 的几个氨基酸取代不会改变抗菌活性。还揭示了 MRSA 总检测脂肪酸中顺式-11-二十碳烯酸的百分比明显高于 MSSA。此外,MRSA 总检测脂肪酸中棕榈酸的百分比趋于低于 MSSA。我们的研究结果将为处理 BMAP-28 对细菌敏感性差异的问题提供新的信息。

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引用本文的文献

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A bovine myeloid antimicrobial peptide (BMAP-28) and its analogs kill pan-drug-resistant Acinetobacter baumannii by interacting with outer membrane protein A (OmpA).一种牛骨髓抗菌肽(BMAP - 28)及其类似物通过与外膜蛋白A(OmpA)相互作用来杀死泛耐药鲍曼不动杆菌。
Medicine (Baltimore). 2018 Oct;97(42):e12832. doi: 10.1097/MD.0000000000012832.