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Background <p>Previous studies have shown that the phosphatidate phosphatase MoPah1 plays a critical role in <i>Magnaporthe oryzae</i> development and pathogenicity. The gene deletion mutant exhibits reduced virulence on rice leaves; however, the MoPah1 regulatory network remains unclear.</p> Result <p>In this study, we applied a quantitative data-independent acquisition approach using the Orbitrap Astral instrument to analyze the gene deletion mutant. We identified 6,799 proteins and 15,682 phosphorylation sites in <i>M. oryzae</i>, with differentially abundant proteins primarily enriched in metabolic and autophagy pathways. Integrating phosphoproteomic and proteomic analyses, we found 72 overlapping proteins. Additionally, we employed glutathione S-transferase pull-down and yeast two-hybrid assays to screen and verify MoPah1-interacting proteins, identifying Pmk1.</p> Conclusions <p>Our findings reveal candidate proteins in the MoPah1 regulatory network and the interaction between MoPah1 and Pmk1 in <i>M. oryzae</i>.</p>

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Orbitrap Astral–based proteome and phosphoproteome analysis identifies candidate proteins associated with the phosphatidate phosphatase MoPah1 in Magnaporthe oryzae

  • 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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  • Juan Zhao,
  • Lili Yang,
  • Xinyi Shi,
  • Xinmei Zou,
  • Bo Liu,
  • Yong Wu,
  • Chengming Zhang,
  • Lan Xiang

摘要

Background

Previous studies have shown that the phosphatidate phosphatase MoPah1 plays a critical role in Magnaporthe oryzae development and pathogenicity. The gene deletion mutant exhibits reduced virulence on rice leaves; however, the MoPah1 regulatory network remains unclear.

Result

In this study, we applied a quantitative data-independent acquisition approach using the Orbitrap Astral instrument to analyze the gene deletion mutant. We identified 6,799 proteins and 15,682 phosphorylation sites in M. oryzae, with differentially abundant proteins primarily enriched in metabolic and autophagy pathways. Integrating phosphoproteomic and proteomic analyses, we found 72 overlapping proteins. Additionally, we employed glutathione S-transferase pull-down and yeast two-hybrid assays to screen and verify MoPah1-interacting proteins, identifying Pmk1.

Conclusions

Our findings reveal candidate proteins in the MoPah1 regulatory network and the interaction between MoPah1 and Pmk1 in M. oryzae.