ArticleMolecular plant pathology2023
Deacetylation of chitin oligomers by Fusarium graminearum polysaccharide deacetylase suppresses plant immunity.
Article in Molecular plant pathology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- FpLaeA Coordinates Fusarium proliferatum Pathogenesis by Orchestrating Mycotoxin Biosynthesis and Host Immune Subversion.Journal of agricultural and food chemistry · 2026Article
- Characterization of the Effector Candidate Repertoire in the Arbuscular Mycorrhizal FungusJournal of fungi (Basel, Switzerland) · 2026Article
- AtLYK4 is the major chitin receptor in Arabidopsis with N-glycosylation and ligand-interacting residues orchestrating chitin perception.Science China. Life sciences · 2026Article
- Plant cell walls as a key driver of plant-pathogen coevolution.FEMS microbiology reviews · 2026Review
- Chitin deacetylases AaCDAs enableMycology · 2026Article
- A putative auxin efflux carrier FgAec1 contributes to the pathogenicity of Fusarium graminearum.BMC biology · 2025Article
- Sustainable antifungal potential of ZnO and MoSWorld journal of microbiology & biotechnology · 2025Article
- A fungal pathogen suppresses host leaf senescence to increase infection.Nature communications · 2025Article
- Deacetylation of chitin oligomers by Fusarium graminearum polysaccharide deacetylase suppresses plant immunity.Molecular plant pathology · 2023Article
- The molecular structure, biological roles, and inhibition of plant pathogenic fungal chitin deacetylases.Frontiers in plant science · 2023Review
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chitin is a long-chain polymer of β-1,4-linked N-acetylglucosamine that forms rigid microfibrils to maintain the hyphal form and protect it from host attacks. Chitin oligomers are first recognized by the plant receptors in the apoplast region, priming the plant's immune system. Here, seven polysaccharide deacetylases (PDAs) were identified and their activities on chitin substrates were investigated via systematic characterization of the PDA family from Fusarium graminearum. Among these PDAs, FgPDA5 was identified as an important virulence factor and was specifically expressed during pathogenesis. ΔFgpda5 compromised the pathogen's ability to infect wheat. The polysaccharide deacetylase structure of FgPDA5 is essential for the pathogenicity of F. graminearum. FgPDA5 formed a homodimer and accumulated in the plant apoplast. In addition, FgPDA5 showed a high affinity toward chitin substrates. FgPDA5-mediated deacetylation of chitin oligomers prevented activation of plant defence responses. Overall, our results identify FgPDA5 as a polysaccharide deacetylase that can prevent chitin-triggered host immunity in plant apoplast through deacetylation of chitin oligomers.
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