ArticleMicrobiology (Reading, England)2011
TagA is a secreted protease of Vibrio cholerae that specifically cleaves mucin glycoproteins.
Article in Microbiology (Reading, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 90 citations in OpenAlex.
- Discovery of a secretedGut microbes · 2026Article
- Intestinal morphology and host‑ and system‑associated microbiome dynamics during short‑term fasting and refeeding of Atlantic salmon in recirculating aquaculture systems.Scientific reports · 2026Article
- Mucin stimulates the growth ofMicrobiology (Reading, England) · 2026Article
- Population structure and phylogenetic analysis of Vibrio cholerae non-O1/O139 by whole genome sequencing.PloS one · 2026Article
- Roles of Glycoconjugates and Mucinases from Carcinogenic Liver Fluke, Opisthorchis viverrini, in Host: Parasite Interactions.Advances in experimental medicine and biology · 2026Review
- Human antibody targetingmBio · 2025Article
- Navigating bacterial motility through chemotaxis: from molecular mechanisms to physiological perspectives.Folia microbiologica · 2025Review
- Mucins and Their Roles in Asthma.Immunological reviews · 2025Review
- Functional divergence of MdpS and MdpS2 reveals mucin-targeting strategies inJournal of oral microbiology · 2025Article
- Characterization of bacteria colonizing the mucosal layer of the gastrointestinal tract of Atlantic salmon farmed in a warm water region.Frontiers in microbiology · 2025Article
- Stepwise assembly and release of Tc toxins from Yersinia entomophaga.Nature microbiology · 2024Article
- Characterization of MdpS: an in-depth analysis of a MUC5B-degrading protease fromFrontiers in microbiology · 2024Article
- Development of a smart pH-responsive nano-polymer drug, 2-methoxy-4-vinylphenol conjugate against the intestinal pathogen, Vibrio cholerae.Scientific reports · 2023Article
- Review
- Stress Responses in Pathogenic Vibrios and Their Role in Host and Environmental Survival.Advances in experimental medicine and biology · 2023Article
- The Role of Nutrients and Nutritional Signals in the Pathogenesis of Vibrio cholerae.Advances in experimental medicine and biology · 2023Article
- Starvation causes changes in the intestinal transcriptome and microbiome that are reversed upon refeeding.BMC genomics · 2022Article
- Secreted Proteases Control the Timing of Aggregative Community Formation in Vibrio cholerae.mBio · 2021Article
- Mucins Dynamics in Physiological and Pathological Conditions.International journal of molecular sciences · 2021Review
- Multiple functions of flagellar motility and chemotaxis in bacterial physiology.FEMS microbiology reviews · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Vibrio cholerae is a human diarrhoeal pathogen that is a major cause of gastrointestinal disease and death worldwide. Pathogenic V. cholerae strains are characterized by the presence of a Vibrio pathogenicity island (VPI) that encodes virulence factors, including the toxin co-regulated pilus (TCP). TagA is encoded within the VPI and is positively co-regulated with cholera toxin and TCP. TagA is a sequelogue of the StcE mucinase of Escherichia coli O157 : H7. We investigated whether this sequence homology reflected a conserved enzymic substrate profile. TagA exhibited metalloprotease activity toward crude purified mucins, salivary mucin and LS174T goblet cell surface mucin. Like StcE, TagA did not cleave general protease substrates, but unlike StcE, TagA did not cleave the mucin-like serpin C1 esterase inhibitor. Both proteins cleaved the immune cell surface mucin CD43, but TagA demonstrated reduced enzymic efficiency relative to StcE. TagA was expressed and secreted by V. cholerae under ToxR-dependent conditions. A tagA-deficient V. cholerae strain showed no defect in a model of in vitro attachment to the HEp-2 cell line; however, overexpression of a proteolytically inactive mutant, TagA(E433D), caused a significant increase in attachment. The increased attachment was reduced by pretreatment of epithelial monolayers with active TagA. Our results indicate that TagA is a mucinase and suggest that TagA may directly modify host cell surface molecules during V. cholerae infection.
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