ArticleMolecular plant pathology2024
An effector SsCVNH promotes the virulence of Sclerotinia sclerotiorum through targeting class III peroxidase AtPRX71.
Article in Molecular plant pathology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
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- Trans-Kingdom sRNA Silencing inPathogens (Basel, Switzerland) · 2025Review
- A Novel Effector FoUpe9 Enhances the Virulence ofJournal of fungi (Basel, Switzerland) · 2025Article
- A Necrotrophic Phytopathogen-Derived GPI-Anchored Protein Functions as an Elicitor to Activate Plant Immunity and Enhance Resistance.Molecular plant pathology · 2025Article
- An effector SsCVNH promotes the virulence of Sclerotinia sclerotiorum through targeting class III peroxidase AtPRX71.Molecular plant pathology · 2024Article
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Many plant pathogens secrete effector proteins into the host plant to suppress host immunity and facilitate pathogen colonization. The necrotrophic pathogen Sclerotinia sclerotiorum causes severe plant diseases and results in enormous economic losses, in which secreted proteins play a crucial role. SsCVNH was previously reported as a secreted protein, and its expression is significantly upregulated at 3 h after inoculation on the host plant. Here, we further demonstrated that deletion of SsCVNH leads to attenuated virulence. Heterologous expression of SsCVNH in Arabidopsis enhanced pathogen infection, inhibited the host PAMP-triggered immunity (PTI) response and increased plant susceptibility to S. sclerotiorum. SsCVNH interacted with class III peroxidase AtPRX71, a positive regulator of innate immunity against plant pathogens. SsCVNH could also interact with other class III peroxidases, thus reducing peroxidase activity and suppressing plant immunity. Our results reveal a new infection strategy employed by S. sclerotiorum in which the fungus suppresses the function of class III peroxidases, the major component of PTI to promote its own infection.
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