Journal of Integrative Agriculture ›› 2026, Vol. 25 ›› Issue (5): 1981-1991.DOI: 10.1016/j.jia.2024.05.023

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FvVam6通过调控液泡结构与形态从而影响轮枝镰孢菌的伏马毒素生物合成

  

  • 收稿日期:2024-02-25 修回日期:2024-05-16 接受日期:2024-04-17 出版日期:2026-05-20 发布日期:2026-04-11

FvVam6 is associated with fungal development and fumonisin biosynthesis via vacuole morphology regulation in Fusarium verticillioides

Jie Liu1, Jie Zhang2, Huijuan Yan3, Tuyong Yi1, Won Bo Shim4#, Zehua Zhou1#   

  1. Hunan Provincial Key Laboratory for Biology and Control of Plant Pests, Hunan Agricultural University, Changsha 410128, China

    College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China

    Department of Microbiology and Immunology, University of California at San Francisco, San Francisco, CA 94143, USA

    Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843, USA


  • Received:2024-02-25 Revised:2024-05-16 Accepted:2024-04-17 Online:2026-05-20 Published:2026-04-11
  • About author:Jie Liu, Tel.: +13618426557, E-mail: 13618426557@stu.hunau.edu.cn; #Correspondence Won Bo Shim, E-mail: wbshim@tamu.edu; Zehua Zhou, E-mail: m15895982813@163.com
  • Supported by:
    This work was supported by the National Natural Science Foundation of China (32202354 to Zehua Zhou) and the Scientific Research Fund of Hunan Provincial Education Department, China (21B0222 to Zehua Zhou).

摘要: 液泡作为真菌细胞内体积最大的多功能动态细胞器,可通过不同膜接触位点与其它细胞器进行交流,进而调控多种细胞过程。作为连接液泡和线粒体的蛋白复合体,液泡-线粒体补片(Vacuole and mitochondria patch, vCLAMP)对于两者间互惠的相互作用至关重要。研究显示,破坏液泡或者线粒体均会显著抑制轮枝镰孢菌的伏马毒素产量。然而蛋白复合体液泡-线粒体补片对于伏马毒素生物合成的调控作用尚不明晰。鉴于此,本研究针对液泡-线粒体补片关键组分FvVam6开展了研究。结果表明,FvVam6参与调控轮枝镰孢菌的生长发育、胁迫响应及致病力。同时我们发现FvVam6缺失突变体的液泡形态畸形,伏马毒素产量显著降低。蛋白序列分析显示,FvVam6蛋白包含一个CNH、一个Clathrin及两个Vps39结构域。进一步通过结构域缺失和表型分析发现,Clathrin及两个Vps39结构域对FvVam6的生物学功能不可或缺,并且ClathrinVps39-2结构域在调控伏马毒素生物合成及致病力中发挥了主要作用。综上所述,本研究揭示了FvVam6通过调控液泡结构与形态从而影响轮枝镰孢菌的伏马毒素生物合成,相关结果有助于促进对我们对液泡-线粒体补片蛋白复合体调控真菌毒素生物合成分子机制的理解。

Abstract: As the largest multifunctional and dynamic organelle in fungi, vacuoles are associated with different organelles through membrane contact sites and participate in various cellular processes.  Vacuole and mitochondria patch (vCLAMP), the membrane contact site that tethers vacuoles and mitochondria, is indispensable for reciprocal interplay between these two organelles.  The impairment of vacuoles and mitochondria significantly suppressed FB1 production in Fusarium verticillioides.  However, the understanding of how vCLAMP complex regulates fumonisin biosynthesis remained unknown.  Herein, the biological functions of vCLAMP component Vam6 were investigated in F. verticillioides. Our results showed that FvVam6 deletion mutant ΔFvVam6 exhibited palpable defects in fungal development, stresses responses and pathogenicity.  In addition, abnormal vacuolar morphology and significantly reduced FB1 production were observed in ΔFvVam6.  Furthermore, we demonstrated that two vacuolar sorting protein 39 (Vps39) domains and clathrin domain were critical for the biological functions of FvVam6, while clathrin and Vps39-2 domains played dominant roles in the regulation of virulence and FB1 production.  Taken together, our results advanced our understanding of vCLAMP in fumonisin biosynthesis in plant pathogenic fungus F. verticillioides.

Key words: Fusarium verticillioides , FvVam6 , fumonisin B1 , vacuolar morphology