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Background <p>In the process of glycolysis and gluconeogenesis, the interconversion between 3-phosphoglyceric acid (3-PGA) and 2-phosphoglyceric acid (2-PGA) is catalyzed by phosphoglycerate mutase (PGAM). Previous research reports indicate that a subclass of the PGAM family, although having sequence homology with the typical PGAMs, lacks PGAM activity and instead participates in biological processes through other mechanisms. Understanding the role of <i>VdPGAM1</i> in the growth and pathogenicity of <i>Verticillium dahliae</i> is essential for elucidating the molecular mechanisms underlying its pathogenicity. In this study, knockout and complementation mutants were successfully obtained through <i>Agrobacterium</i>-mediated transformation (ATMT) technology. Wild-type (WT), knockout mutants, and complementation mutants were all used to study the function of <i>VdPGAM1</i>.</p> Results <p>Enzyme activity assays, pyruvate content measurement, and the utilization of different carbon sources all suggest that VdPGAM1 protein lacks PGAM activity. A series of experiments, including the glass paper penetration test, spore detection, and electron microscopy observation, demonstrate that VdPGAM1 is involved in mycelial growth, penetration, and spore production. The <i>VdPGAM1</i> gene knockout mutant exhibits enhanced resistance to abiotic stress, with reduced microspore and melanin content, and enhanced resistance to oxidative stress. The yeast two-hybrid assay (Y2H) and the luciferase complementation imaging assay (LCI) demonstrated that VdPGAM1 can interact with the adhesion protein VdFAS1. Furthermore, these mutants displayed increased hydrophobicity and adhesion ability, suggesting that <i>VdPGAM1</i> negatively regulates the pathogenicity of <i>V. dahliae</i> to cotton.</p> Conclusion <p><i>VdPGAM1</i> is involved in the growth of <i>V. dahliae</i> and its response to abiotic stress. Combining the results of the virulence assay, RNA sequencing, and Y2H experiments, we confirmed that <i>VdPGAM1</i> negatively regulates virulence. Additionally, we hypothesized that the interaction between VdPGAM1 and the adhesin VdFAS1 might play a crucial role.</p>

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The vital role of VdPGAM1 in Verticillium dahliae growth, stress resistance, adhesion and virulence

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月2日

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  • Li Dongpo,
  • Chen Luqi,
  • Zhang Yalin,
  • Zhu Heqin,
  • Tian Liwen,
  • Wei Feng,
  • Zhao Lihong,
  • Feng Hongjie,
  • Zhao Jun,
  • Feng Zili,
  • Zhou Jinglong

摘要

Background

In the process of glycolysis and gluconeogenesis, the interconversion between 3-phosphoglyceric acid (3-PGA) and 2-phosphoglyceric acid (2-PGA) is catalyzed by phosphoglycerate mutase (PGAM). Previous research reports indicate that a subclass of the PGAM family, although having sequence homology with the typical PGAMs, lacks PGAM activity and instead participates in biological processes through other mechanisms. Understanding the role of VdPGAM1 in the growth and pathogenicity of Verticillium dahliae is essential for elucidating the molecular mechanisms underlying its pathogenicity. In this study, knockout and complementation mutants were successfully obtained through Agrobacterium-mediated transformation (ATMT) technology. Wild-type (WT), knockout mutants, and complementation mutants were all used to study the function of VdPGAM1.

Results

Enzyme activity assays, pyruvate content measurement, and the utilization of different carbon sources all suggest that VdPGAM1 protein lacks PGAM activity. A series of experiments, including the glass paper penetration test, spore detection, and electron microscopy observation, demonstrate that VdPGAM1 is involved in mycelial growth, penetration, and spore production. The VdPGAM1 gene knockout mutant exhibits enhanced resistance to abiotic stress, with reduced microspore and melanin content, and enhanced resistance to oxidative stress. The yeast two-hybrid assay (Y2H) and the luciferase complementation imaging assay (LCI) demonstrated that VdPGAM1 can interact with the adhesion protein VdFAS1. Furthermore, these mutants displayed increased hydrophobicity and adhesion ability, suggesting that VdPGAM1 negatively regulates the pathogenicity of V. dahliae to cotton.

Conclusion

VdPGAM1 is involved in the growth of V. dahliae and its response to abiotic stress. Combining the results of the virulence assay, RNA sequencing, and Y2H experiments, we confirmed that VdPGAM1 negatively regulates virulence. Additionally, we hypothesized that the interaction between VdPGAM1 and the adhesin VdFAS1 might play a crucial role.