ArticleNature communications2025
Enzymatic oxidation of galacturonides from pectin breakdown contributes to stealth infection by Oomycota phytopathogens.
Article in Nature communications, 2025. 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.
- Transcriptome study ofMicrobiology spectrum · 2026Article
- Enzymatically hydrolyzed oligosaccharide fingerprinting using nanopipettes at the single-molecule level.Chemical science · 2026Article
- Structural insights into glycan recognition by plant immune receptors: a comparative perspective with animal innate immune systems.The Plant journal : for cell and molecular biology · 2026Review
- Utilizing bulk and single-cell RNA sequencing to identify potential biomarkers linked to angiogenesis and integrated stress response in chondrosarcoma.Scientific reports · 2026Article
- Plant cell walls as a key driver of plant-pathogen coevolution.FEMS microbiology reviews · 2026Review
- Selected cell wall-associated components in plant defense responses against microbial pathogens.Frontiers in plant science · 2026Review
- Host microenvironment in potato-Phytophthora infestans interaction revealed by single-cell spatiotemporal transcriptome.Nature plants · 2026Article
- Oligosaccharide elicitors in plant immunity: Molecular mechanisms and disease resistance strategies.Plant communications · 2025Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Oomycetes manipulate plant innate immunity through galacturonide oxidases.Nature communications · 2025Article
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
Phytophthora phytopathogens from Oomycota cause devastating crop losses and threaten food security. However, Phytophthora secreted proteins that interact with plant-hosts remain underexplored. Here, auxiliary activity family 7 (AA7) enzymes from Ascomycota and Oomycota phytopathogens were shown to oxidise pectin-derived galacturonic acid and/or oligogalacturonides (OGs). Unique mono-cysteinyl-FAD oxidases with positively-charged active sites, suited to oxidise OGs, were discovered in Phytophthora sojae. The P. sojae OG oxidase genes, prevalent in this genus, were co-transcribed with pectin-degradation counterparts during early infection of soybean. Single OG oxidase knockouts significantly decreased P. sojae biomass in planta, potentially linking OG oxidases to virulence. We propose that oxidation by AA7 enzymes impairs the elicitor activity of OGs, potentially contributing to stealth Oomycota infection. Oxidation of OGs unravels a previously unknown microbial mechanism that contributes to evade plant immune-response against pathogens. Our findings highlight a unique oxidase architecture and hitherto unexplored targets for bioprotection from major plant pathogens.
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