以小麦锌结合蛋白 TaZnBP 为靶标的锌金属蛋白酶 FgM35 对禾谷镰刀菌的毒力有促进作用。

Xin-Tong Wang, Kou-Han Liu, Ying Li, Yan-Yan Ren, Qiang Li, Bao-Tong Wang
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引用次数: 0

摘要

金属蛋白酶在生物体内无处不在。病原微生物分泌的大多数金属蛋白酶也被称为毒力因子,因为它们能降解宿主外部组织中的蛋白质,从而降低宿主的免疫力,增加宿主对疾病的易感性。锌金属蛋白酶是最常见的金属蛋白酶之一。在我们的报告中,我们研究了锌金属蛋白酶 FgM35 在禾谷镰刀菌中的生物学功能以及感染过程中病原体与宿主的相互作用。我们发现,缺失突变体ΔFgM35的无性繁殖和有性生殖均受到影响,禾谷镰刀菌对金属胁迫的耐受性也受到影响。此外,FgM35 的缺失还降低了禾谷镰孢的毒力。利用小麦酵母 cDNA 文库筛选了小麦靶标 TaZnBP,并通过 HADDOCK 分子对接、酵母双杂交、Bi-FC、Luc 和 Co-IP 试验验证了 FgM35 与 TaZnBP 之间的相互作用。同时还证明了 TaZnBP 对植物免疫的贡献。总之,我们的研究揭示了 FgM35 在禾谷镰孢的繁殖过程和致病性中不可或缺的作用,并确定了 FgM35 与 TaZnBP 之间的相互作用以及 TaZnBP 的功能。这为进一步研究金属蛋白酶在病原体-宿主相互作用中的功能提供了理论依据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Zinc metalloprotease FgM35, which targets the wheat zinc-binding protein TaZnBP, contributes to the virulence of Fusarium graminearum.

Metalloproteinases are ubiquitous in organisms. Most metalloproteinases secreted by pathogenic microorganisms are also called virulence factors, because they degrade proteins in the external tissues of the host, thereby reducing the host's immunity and increasing its susceptibility to disease. Zinc metalloproteinase is one of the most common metalloproteinases. In our report, we studied the biological function of zinc metalloprotease FgM35 in Fusarium graminearum and the pathogen-host interaction during infection. We found that the asexual and sexual reproduction of the deletion mutant ΔFgM35 were affected, as well as the tolerance of F. graminearum to metal stress. In addition, deletion of FgM35 reduced the virulence of F. graminearum. The wheat target TaZnBP was screened using a wheat yeast cDNA library, and the interaction between FgM35 and TaZnBP was verified by HADDOCK molecular docking, yeast two-hybrid, Bi-FC, Luc, and Co-IP assays. The contribution of TaZnBP to plant immunity was also demonstrated. In summary, our work revealed the indispensable role of FgM35 in the reproductive process and the pathogenicity of F. graminearum, and it identified the interaction between FgM35 and TaZnBP as well as the function of TaZnBP. This provides a theoretical basis for further study of the function of metalloproteinases in pathogen-host interactions.

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