ArticleNature communications2024
Arabidopsis SBT5.2 and SBT1.7 subtilases mediate C-terminal cleavage of flg22 epitope from bacterial flagellin.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Mechanisms and balanced regulation of plant immunity.Nature reviews. Molecular cell biology · 2026Review
- Diverse phytocytokines derived from conserved subtilase scaffolds co-evolved with clustered receptors to confer defence responses in legumes.Nature plants · 2026Article
- A Phytosulfokine signaling module activates the Nod factor receptor to control soybean nodulation.Nature communications · 2026Article
- Constitutive and inducible oleoresin defenses share genetic architectures and mechanisms in Pinus taeda.The New phytologist · 2026Article
- Subtilase-mediated maturation of EPF1 and EPF2 is crucial for stomatal patterning.Nature plants · 2026Article
- Plant subtilases as key initiators of peptide ligand-receptor signaling.The Plant journal : for cell and molecular biology · 2026Review
- Orchestration of plant PRR- and NLR-mediated immunity: Protein kinases and beyond.Molecular cell · 2025Review
- Silenced cutters: mechanisms and effects of protease inhibition in plant-pathogen interactions.Journal of experimental botany · 2025Review
- Four guidelines to identify bona fide protease-substrate pairs.Journal of experimental botany · 2025Review
- Unlocking expanded flagellin perception through rational receptor engineering.Nature plants · 2025Article
- mamp-ml: A deep learning approach to epitope immunogenicity in plants.bioRxiv : the preprint server for biology · 2025Article
- Flagellin sensing, signaling, and immune responses in plants.Plant communications · 2025Review
- Streamline Protocol forPlant direct · 2025Article
- An Activity-Based Proteomics with Two-Dimensional Polyacrylamide Gel Electrophoresis (2D-PAGE) for Identifying Target Proteases inBio-protocol · 2025Article
- Proteasomes accumulate in the plant apoplast where they participate in microbe-associated molecular pattern (MAMP)-triggered pathogen defense.Nature communications · 2025Article
- Peptide hormones in plants.Molecular horticulture · 2025Review
- Plant Pattern recognition receptors: Exploring their evolution, diversification, and spatiotemporal regulation.Current opinion in plant biology · 2024Article
- Subtilase SBT5.2 inactivates flagellin immunogenicity in the plant apoplast.Nature communications · 2024Article
- Extracellular plant subtilases dampen cold-shock peptide elicitor levels.Nature plants · 2024Article
- Xylem Sap Proteome Analysis Provides Insight into Root-Shoot Communication in Response to flg22.Plants (Basel, Switzerland) · 2024Article
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7 authors.
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Abstract
Plants initiate specific defense responses by recognizing conserved epitope peptides within the flagellin proteins derived from bacteria. Proteolytic cleavage of epitope peptides from flagellin by plant apoplastic proteases is thought to be crucial for the perception of the epitope by the plant receptor. However, the identity of the plant proteases involved in this process remains unknown. Here, we establish an efficient identification system for the target proteases in Arabidopsis apoplastic fluid; the method employs native two-dimensional electrophoresis followed by an in-gel proteolytic assay using a fluorescence-quenching peptide substrate. We designed a substrate to specifically detect proteolytic activity at the C-terminus of the flg22 epitope in flagellin and identified two plant subtilases, SBT5.2 and SBT1.7, as specific proteases responsible for the C-terminal cleavage of flg22. In the apoplastic fluid of Arabidopsis mutant plants deficient in these two proteases, we observe a decrease in the C-terminal cleavage of the flg22 domain from flagellin, leading to a decrease in the efficiency of flg22 epitope liberation. Consequently, defensive reactive oxygen species (ROS) production is delayed in sbt5.2 sbt1.7 double-mutant leaf disks compared to wild type following flagellin exposure.
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