ArticleThe Journal of biological chemistry2011
Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 125 citations in OpenAlex.
- Substrate secretion by different EHEC secretion systems during their interaction with epithelial cells.Virulence · 2026Article
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inJournal of bacteriology · 2026Article
- The GlyGly-CTERM domain functions as an independent motif that targets proteins to rhombosortase inbioRxiv : the preprint server for biology · 2026Article
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- The Type II Secretion System Utilizes AsmA-like Protein GspN to Facilitate Transport of Lipoproteins to the Cell Surface inbioRxiv : the preprint server for biology · 2025Article
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
- Hemagglutinin Protease HapA Associated With Vibrio cholerae Outer Membrane Vesicles (OMVs) Disrupts Tight and Adherens Junctions.Journal of extracellular vesicles · 2025Article
- Myxosortase: an intramembrane protease that sorts MYXO-CTERM proteins to the cell surface.mBio · 2025Article
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- The intersection between host-pathogen interactions and metabolism during Vibrio cholerae infection.Current opinion in microbiology · 2024Review
- Identification of Effectors: Precipitation of Supernatant Material.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Bacterial Chitinases and Their Role in Human Infection.Infection and immunity · 2023Review
- Mechanism of secretion of TcpF by theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Uncovering the Secretion Systems ofAntibiotics (Basel, Switzerland) · 2023Review
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- Comparative genomics and transcriptomics insight into myxobacterial metabolism potentials and multiple predatory strategies.Frontiers in microbiology · 2023Article
- RpoN is required for the motility and contributes to the killing ability of Plesiomonas shigelloides.BMC microbiology · 2022Article
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- Secreted Proteases Control the Timing of Aggregative Community Formation in Vibrio cholerae.mBio · 2021Article
- Coral mucus rapidly induces chemokinesis and genome-wide transcriptional shifts toward early pathogenesis in a bacterial coral pathogen.The ISME journal · 2021Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The type II secretion (T2S) system is responsible for extracellular secretion of a broad range of proteins, including toxins and degradative enzymes that play important roles in the pathogenesis and life cycle of many gram-negative bacteria. In Vibrio cholerae, the etiological agent of cholera, the T2S machinery transports cholera toxin, which induces profuse watery diarrhea, a hallmark of this life-threatening disease. Besides cholera toxin, four other proteins have been shown to be transported by the T2S machinery, including hemagglutinin protease, chitinase, GbpA, and lipase. Here, for the first time, we have applied proteomic approaches, including isotope tagging for relative and absolute quantification coupled with multidimensional liquid chromatography and tandem mass spectrometry, to perform an unbiased and comprehensive analysis of proteins secreted by the T2S apparatus of the V. cholerae El Tor strain N16961 under standard laboratory growth conditions. This analysis identified 16 new putative T2S substrates, including sialidase, several proteins participating in chitin utilization, two aminopeptidases, TagA-related protein, cytolysin, RbmC, three hypothetical proteins encoded by VCA0583, VCA0738, and VC2298, and three serine proteases VesA, VesB, and VesC. Focusing on the initial characterization of VesA, VesB, and VesC, we have confirmed enzymatic activities and T2S-dependent transport for each of these proteases. In addition, analysis of single, double, and triple protease knock-out strains indicated that VesA is the primary protease responsible for processing the A subunit of cholera toxin during in vitro growth of the V. cholerae strain N16961.
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