Resistance response to Arenicin derivatives in Escherichia coli

文献类型： 外文期刊

第一作者： Wang, Zhenlong

作者： Wang, Zhenlong;Yang, Na;Teng, Da;Hao, Ya;Li, Ting;Han, Huihui;Mao, Ruoyu;Wang, Jianhua;Wang, Zhenlong;Yang, Na;Teng, Da;Hao, Ya;Li, Ting;Han, Huihui;Mao, Ruoyu;Wang, Jianhua

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关键词： Antimicrobial peptide resistance; N6NH(2); MDR; Fitness; Mechanisms of resistance

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：5.56； 五年影响因子：5.365 ）

ISSN： 0175-7598

年卷期： 2022 年 106 卷 1 期

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收录情况： SCI

摘要： The rising prevalence of antibiotic resistance poses the greatest health threats. Antimicrobial peptides (AMPs) are regarded as the potentially effective therapy. To avoid current crisis of antibiotic resistance, a comprehensive understanding of AMP resistance is necessary before clinical application. In this study, the development of resistance to the anti-Gram-negative bacteria peptide N6NH(2) (21 residues, beta-sheet) was characterized in E. coli ATCC25922. Three N6NH(2)-resistant E. coli mutants with 32-fold increase in MIC were isolated by serially passaging bacterial lineages in progressively increasing concentrations of N6NH(2) and we mainly focus on the phenotype of N6NH(2)-resistant bacteria different from sensitive bacteria. The results showed that the resistance mechanism was attributed to synergy effect of multiple mechanisms: (i) increase biofilm formation capacity (3 similar to 4-fold); (ii) weaken the affinity of lipopolysaccharide (LPS) with N6NH(2) (3 similar to 8-fold); and (iii) change the cell membrane permeability and potential. Interestingly, a chimeric peptide-G6, also a N6NH(2) analog, which keep the same antibacterial activity to both wild-type and resistant clones (MIC value: 16 mu g/mL), could curb N6NH(2)-resistant mutants by stronger inhibition of biofilm formation, stronger affinity with LPS, and stronger membrane permeability and depolarization than that of N6NH(2).

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