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Isoflavone glucoside genistin, an inhibitor targeting Sortase A and Listeriolysin O, attenuates the virulence of Listeria monocytogenes in vivo and in vitro

文献类型： 外文期刊

作者： Liu, Minda 1 ; Lv, Qianghua 1 ; Xu, Jingwen 1 ; Liu, Baichen 4 ; Zhou, Yonglin 1 ; Zhang, Siqi 1 ; Shen, Xue 1 ; Wang, Lin 1 ;

作者机构： 1.Jilin Univ, Inst Zoonosis, Coll Vet Med, State Key Lab Zoonot Dis,Key Lab Zoonosis Res,Mini, Changchun, Peoples R China

2.Jilin Univ, Coll Food Sci & Engn, Dept Food Sci, Changchun, Peoples R China

3.First Hosp Jilin Univ, Dept Resp Med, Changchun, Peoples R China

4.Jilin Univ, Bethune Clin Med Coll 2, Changchun 130012, Jilin, Peoples R China

5.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Jinan, Peoples R China

6.Key Lab Livestock & Poultry Multiom MARA, Jinan, Peoples R China

7.Jilin Univ, Coll Vet Med, Linyuan St, Changchun 130000, Jilin, Peoples R China

关键词： Listeria monocytogenes; Sortase A; Listeriolysin O; Antiinfection; Antivirulence

期刊名称：BIOCHEMICAL PHARMACOLOGY （ 影响因子：5.8； 五年影响因子：5.8 ）

ISSN： 0006-2952

年卷期： 2023 年 209 卷

页码：

收录情况： SCI

摘要： As a common intracellular facultative anaerobic Gram-positive bacterium, Listeria monocytogenes (L. monocytogenes) exhibits strong resistance to extreme environments, such as low temperature and a wide range of pH values, causing contamination in food production and processing. Sortase A (SrtA) and listeriolysin O (LLO), two crucial virulence factors of L. monocytogenes, are widely recognized as potential targets for the development of anti-L. monocytogenes infection drugs. In this study, we found that genistin simultaneously inhibits the peptidase activity of SrtA and the hemolytic activity of LLO without affecting the growth of L. monocytogenes, alleviating concerns about developing resistance. Furthermore, we demonstrated that genistin reduces L. monocytogenes biofilm formation and invasion of human colorectal cancer (Caco-2) cells. Subsequent mechanistic studies revealed that genistin inhibited LLO-mediated Caco-2 cell damage by blocking LLO oligomerization. Fluorescence quenching assay revealed the potential binding mode of SrtA and LLO to genistin. Genistin might bind to the active pocket of SrtA through residues Leu33, Asn29, and Met40, interacting with D1 domain of LLO involved in oligomerization and pore formation through residues Asn259. Studies in infection models revealed that genistin reduces mortality and pathological damage in mice infected with L. monocytogenes. These results indicate that genistin is a promising anti-virulence agent that could be considered an alternative candidate for the treatment of L. monocytogenes infection.

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