ArticleJournal of bacteriology2015
Xanthomonas campestris pv. vesicatoria Secretes Proteases and Xylanases via the Xps Type II Secretion System and Outer Membrane Vesicles.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 102 citations in OpenAlex.
- Genomic and enzymatic signatures underlying lifestyle diversity inMicrobial genomics · 2026Article
- Guardians or Gateways? The Intricate Relationship Between Plant Cell Walls and Pathogenic Xanthomonas.Molecular plant pathology · 2026Review
- Plant cell wall remodeling and peptide signaling under abiotic and biotic stress.Plant communications · 2026Review
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- Bacterial extracellular vesicles as players in biofilm dynamics and community interactions.FEMS microbiology reviews · 2026Review
- Functional and proteomic characterization ofFrontiers in plant science · 2026Article
- Toward a better understanding of the ecological roles of extracellular vesicles from plant-associated bacteria.Applied and environmental microbiology · 2025Review
- Expanding Horizons: Next-Generation and Interdisciplinary Advances in the Applications of Extracellular Vesicles.Journal of extracellular biology · 2025Review
- Bacterial alarmone (p)ppGpp mediates the pathogenicity ofmSystems · 2025Article
- Secreted LysM proteins are required for niche competition and full virulence in Pseudomonas savastanoi during host plant infection.PLoS pathogens · 2025Article
- Functional Cargo in Membrane Vesicles From a Citrus Pathogen.Environmental microbiology reports · 2025Article
- Review
- Modularization of the type II secretion gene cluster from Xanthomonas euvesicatoria facilitates the identification of a structurally conserved XpsCLM assembly platform complex.PLoS pathogens · 2025Article
- Membrane Vesicles Can Contribute to Cellulose Degradation by Teredinibacter turnerae, a Cultivable Intracellular Endosymbiont of Shipworms.Microbial biotechnology · 2024Article
- Comparative genomics-based insights intoApplied and environmental microbiology · 2024Article
- Membrane vesicles can contribute to cellulose degradation bybioRxiv : the preprint server for biology · 2024Article
- Insights into Bacterial Extracellular Vesicle Biogenesis, Functions, and Implications in Plant-Microbe Interactions.Microorganisms · 2024Review
- Leaf microbiome dysbiosis triggered by T2SS-dependent enzyme secretion from opportunistic Xanthomonas pathogens.Nature microbiology · 2024Article
- Bacterial membrane vesicles: orchestrators of interkingdom interactions in microbial communities for environmental adaptation and pathogenic dynamics.Frontiers in immunology · 2024Review
- Membrane vesicle engineering with "à la carte" bacterial-immunogenic molecules for organism-free plant vaccination.Microbial biotechnology · 2023Review
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledMany plant-pathogenic bacteria utilize type II secretion (T2S) systems to secrete degradative enzymes into the extracellular milieu. T2S substrates presumably mediate the degradation of plant cell wall components during the host-pathogen interaction and thus promote bacterial virulence. Previously, the Xps-T2S system from Xanthomonas campestris pv. vesicatoria was shown to contribute to extracellular protease activity and the secretion of a virulence-associated xylanase. The identities and functions of additional T2S substrates from X. campestris pv. vesicatoria, however, are still unknown. In the present study, the analysis of 25 candidate proteins from X. campestris pv. vesicatoria led to the identification of two type II secreted predicted xylanases, a putative protease and a lipase which was previously identified as a virulence factor of X. campestris pv. vesicatoria. Studies with mutant strains revealed that the identified xylanases and the protease contribute to virulence and in planta growth of X. campestris pv. vesicatoria. When analyzed in the related pathogen X. campestris pv. campestris, several T2S substrates from X. campestris pv. vesicatoria were secreted independently of the T2S systems, presumably because of differences in the T2S substrate specificities of the two pathogens. Furthermore, in X. campestris pv. vesicatoria T2S mutants, secretion of T2S substrates was not completely absent, suggesting the contribution of additional transport systems to protein secretion. In line with this hypothesis, T2S substrates were detected in outer membrane vesicles, which were frequently observed for X. campestris pv. vesicatoria. We, therefore, propose that extracellular virulence-associated enzymes from X. campestris pv. vesicatoria are targeted to the Xps-T2S system and to outer membrane vesicles. IMPORTANCE: The virulence of plant-pathogenic bacteria often depends on TS2 systems, which secrete degradative enzymes into the extracellular milieu. T2S substrates are being studied in several plant-pathogenic bacteria, including Xanthomonas campestris pv. vesicatoria, which causes bacterial spot disease in tomato and pepper. Here, we show that the T2S system from X. campestris pv. vesicatoria secretes virulence-associated xylanases, a predicted protease, and a lipase. Secretion assays with the related pathogen X. campestris pv. campestris revealed important differences in the T2S substrate specificities of the two pathogens. Furthermore, electron microscopy showed that T2S substrates from X. campestris pv. vesicatoria are targeted to outer membrane vesicles (OMVs). Our results, therefore, suggest that OMVs provide an alternative transport route for type II secreted extracellular enzymes.
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