ArticleThe New phytologist2024
Activity-based proteomics uncovers suppressed hydrolases and a neo-functionalised antibacterial enzyme at the plant-pathogen interface.
Article in The New phytologist, 2024. 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, 28 citations in OpenAlex.
- NbRD21 protease controls receptor kinase homeostasis in Nicotiana benthamiana.The New phytologist · 2026Article
- Processing and release of the maize phytocytokine Zip1.Plant physiology · 2026Article
- Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026Review
- Review
- Protein-Derived Signal Peptides Induced by Agrobacterium Infection Promote the Secretion of Recombinant Proteins in Nicotiana benthamiana.Plant biotechnology journal · 2026Article
- Apoplastic proteomic reveals Colletotrichum fructicola effector CfXyn11A recognized by tobacco and suppressed by pear in the apoplast.Molecular horticulture · 2025Article
- Extracellular plant subtilases dampen cold-shock peptide elicitor levels.Nature plants · 2024Article
- Proteolysis in plant immunity.The Plant cell · 2024Review
- Comprehensive genome-wide analysis of wheat xylanase inhibitor protein (XIP) genes: unveiling their role in Fusarium head blight resistance and plant immune mechanisms.BMC plant biology · 2024Article
- AlphaFold-Multimer predicts cross-kingdom interactions at the plant-pathogen interface.Nature communications · 2023Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
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Abstract
The extracellular space of plant tissues contains hundreds of hydrolases that might harm colonising microbes. Successful pathogens may suppress these hydrolases to enable disease. Here, we report the dynamics of extracellular hydrolases in Nicotiana benthamiana upon infection with Pseudomonas syringae. Using activity-based proteomics with a cocktail of biotinylated probes, we simultaneously monitored 171 active hydrolases, including 109 serine hydrolases (SHs), 49 glycosidases (GHs) and 13 cysteine proteases (CPs). The activity of 82 of these hydrolases (mostly SHs) increases during infection, while the activity of 60 hydrolases (mostly GHs and CPs) is suppressed during infection. Active β-galactosidase-1 (BGAL1) is amongst the suppressed hydrolases, consistent with production of the BGAL1 inhibitor by P. syringae. One of the other suppressed hydrolases, the pathogenesis-related NbPR3, decreases bacterial growth when transiently overexpressed. This is dependent on its active site, revealing a role for NbPR3 activity in antibacterial immunity. Despite being annotated as a chitinase, NbPR3 does not possess chitinase activity and contains an E112Q active site substitution that is essential for antibacterial activity and is present only in Nicotiana species. This study introduces a powerful approach to reveal novel components of extracellular immunity, exemplified by the discovery of the suppression of neo-functionalised Nicotiana-specific antibacterial NbPR3.
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