c-di-GMP modulates type IV MSHA pilus retraction and surface attachment in Vibrio cholerae
c-di-GMP modulates type IV MSHA pilus retraction and surface attachment in Vibrio cholerae
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DOI：
10.1038/s41467-020-15331-8
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发表时间：
2020-03-25
影响因子：
16.6
通讯作者：
Yildiz, Fitnat H.
中科院分区：
文献类型：
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作者：
Floyd, Kyle A.;Lee, Calvin K.;Yildiz, Fitnat H.
霍乱弧菌形成的生物膜促进了环境持久性和宿主体内的高度感染性。生物膜的形成受3 '，5'-环二鸟苷酸（c-di-GMP）调节，并需要产生IV型甘露糖敏感性血凝素（MSHA）菌毛。在这里，我们表明，MSHA菌毛是一个动态的可伸缩系统，其活动直接由c-di-GMP控制。c-di-GMP和ATP酶MshE之间的相互作用促进菌毛延伸，而低水平的c-di-GMP与增强的收缩相关。由ATP酶PilT促进的收缩的损失增加近表面漫游运动，并损害初始表面附着。然而，表面附着后的长时间回缩导致MSHA介导的表面锚定减少和脱离水平增加。我们的研究结果表明，c-di-GMP直接控制MshE活性，从而调节MSHA菌毛延伸和收缩动力学，并调节霍乱弧菌表面附着和定殖。霍乱弧菌的生物膜形成受c-di-GMP调节，需要IV型MSHA菌毛。在此，弗洛伊德等人表明MSHA菌毛是一个动态系统，并且伸展和回缩都直接由c-di-GMP通过调节伸展ATP酶MshE的活性来控制。
Biofilm formation by Vibrio cholerae facilitates environmental persistence, and hyperinfectivity within the host. Biofilm formation is regulated by 3',5'-cyclic diguanylate (c-di-GMP) and requires production of the type IV mannose-sensitive hemagglutinin (MSHA) pilus. Here, we show that the MSHA pilus is a dynamic extendable and retractable system, and its activity is directly controlled by c-di-GMP. The interaction between c-di-GMP and the ATPase MshE promotes pilus extension, whereas low levels of c-di-GMP correlate with enhanced retraction. Loss of retraction facilitated by the ATPase PilT increases near-surface roaming motility, and impairs initial surface attachment. However, prolonged retraction upon surface attachment results in reduced MSHA-mediated surface anchoring and increased levels of detachment. Our results indicate that c-di-GMP directly controls MshE activity, thus regulating MSHA pilus extension and retraction dynamics, and modulating V. cholerae surface attachment and colonization. Biofilm formation by Vibrio cholerae is regulated by c-di-GMP and requires the type IV MSHA pilus. Here, Floyd et al. show that the MSHA pilus is a dynamic system, and that both extension and retraction are directly controlled by c-di-GMP via regulation of activity of the extension ATPase MshE.