ArticleNature plants2024
Extracellular plant subtilases dampen cold-shock peptide elicitor levels.
Article in Nature plants, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Diverse phytocytokines derived from conserved subtilase scaffolds co-evolved with clustered receptors to confer defence responses in legumes.Nature plants · 2026Article
- Diversity of Soil Fungi, Entomopathogenic Fungi and Their Driving Factors in the Eastern Tanggula Mountains in the Qinghai-Tibet Plateau.Microorganisms · 2026Article
- A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Pathogen-inspired engineering of plant protease enhances late blight resistance.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-wide identification and characterization of Subtilisin-like Serine protease encoding genes in Vigna radiata L. Wilczek.Scientific reports · 2025Article
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7 authors.
Funding
Abstract
Recognizing pathogen-associated molecular patterns on the cell surface is crucial for plant immunity. The proteinaceous nature of many of these patterns suggests that secreted proteases play important roles in their formation and stability. Here we demonstrate that the apoplastic subtilase SBT5.2a inactivates the immunogenicity of cold-shock proteins (CSPs) of the bacterial plant pathogen Pseudomonas syringae by cleaving within the immunogenic csp22 epitope. Consequently, mutant plants lacking SBT5.2a activity retain higher levels of csp22, leading to enhanced immune responses and reduced pathogen growth. SBT5.2 sensitivity is influenced by sequence variation surrounding the cleavage site and probably extends to CSPs from other bacterial species. These findings suggest that variations in csp22 stability among bacterial pathogens are a crucial factor in plant-bacteria interactions and that pathogens exploit plant proteases to avoid pattern recognition.
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