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H2S-mediated S-sulfhydration coordinates autophagy and infection of the rice blast fungus

ABSTRACT: Hydrogen sulfide (H2S), a potent signaling molecule, regulates cellular activities in plants and mammals through S-sulfhydration, a post-translational modification. The role of H2S and its molecular targets in fungi, however, remain unclear. Our study demonstrates that H2S, synthesized by cystathionine γ-lyase (CSE1) in the rice blast fungus Magnaporthe oryzae, is essential for optimal fungal infection. Excessive H2S, through S-sulfhydration, impairs fungal infectivity by negatively regulating autophagy. Using quantitative proteomics, we identified numerous S-sulfhydrated proteins in M. oryzae, including the autophagy-related protein ATG18. We found that S-sulfhydration of a critical cysteine residue (Cys78) in ATG18 is essential for its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P), thereby maintaining the protein's structural stability and regulating autophagy. This study uncovers a new mechanism by which H2S-mediated S-sulfhydration controls autophagy in pathogenic fungi, and suggests the potential use of H2S donors as a strategy to control fungal diseases by targeting fungal development and infection structures, with broad implications for agriculture and disease management.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Oryza Sativa (rice)

TISSUE(S): Mycelial Cord

SUBMITTER: hong Hu

LAB HEAD: Xiao-Lin Chen

PROVIDER: PXD063170 | Pride | 2025-06-12

REPOSITORIES: Pride

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			Action	DRS
	RE334LP_CSE_OE_4_Slot1-26_1_12395.d.zip	Other
	RE334LP_CSE_OE_5_Slot1-27_1_12397.d.zip	Other
	RE334LP_P131_1_Slot1-28_1_12399.d.zip	Other
	RE334LP_P131_2_Slot1-29_1_12401.d.zip	Other
	RE334LQ_CSE_OE_4_Slot1-41_1_20487.d.zip	Other

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