Vibrio cholerae hemagglutinin(HA)/protease: An extracellular metalloprotease with multiple pathogenic activities
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Vibrio cholerae of serogroup O1 and O139, the etiological agent of the diarrheal disease cholera, expresses the extracellular Zn-dependent metalloprotease hemagglutinin (HA)/protease also reported as vibriolysin. This enzyme is also produced by non-O1/O139 (non-cholera) strains that cause mild, sporadic illness (i.e. gastroenteritis, wound or ear infections). Orthologs of HA/protease are present in other members of the Vibrionaceae family pathogenic to humans and fish. HA/protease belongs to the M4 neutral peptidase family and displays significant amino acid sequence homology to Pseudomonas aeruginosa elastase (LasB) and Bacillus thermoproteolyticus thermolysin. It exhibits a broad range of potentially pathogenic activities in cell culture and animal models. These activities range from the covalent modification of other toxins, the degradation of the protective mucus barrier and disruption of intestinal tight junctions. Here we review (i) the structure and regulation of HA/protease expression, (ii) its interaction with other toxins and the intestinal mucosa and (iii) discuss the possible role(s) of HA/protease in the pathogenesis of cholera.
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The extracellular Zn-dependent metalloprotease hemagglutinin (vibriolysin) has been implicated in the pathogenicity of Vibrio cholerae.
“The extracellular Zn-dependent metalloprotease hemagglutinin (HA) also called vibriolysin, has been implicated in the pathogenicity of Vibrio cholerae.”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [10]
Proteases from infectious agents such as Pic in diarrheagenic E. coli and Shigella, or vibriolysin in V. cholera, degrade colonic mucus, which is a key step facilitating epithelium invasion.
“Proteases from different infectious agents such as Pic in diarrheagenic E. coli and Shigella, or vibriolysin in V. cholera, degrade the colonic mucus, which is a key step facilitating epithelium invasion.10,68,69,71”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [10]
Vibriolysin presents a broad range of potentially pathogenic activities including degradation of the mucus barrier or disruption of epithelial tight junctions.
“vibriolysin presents a broad range of potentially pathogenic activities including degradation of the mucus barrier or disruption of epithelial tight junctions.10,83”
From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [10]
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- Authors
- Benitez, J. A., & Silva, A. J.
- Affiliations
- Morehouse School of Medicine (US)
- Corresponding author
- Silva, Anisia J.
- ORCID
- Silva, Anisia J.
- Venue
- Toxicon
- Publisher
- Elsevier BV
- Published
- 2016-06
- Volume
- 115
- Pages
- 55-62
- ISSN
- 0041-0101 (ISSN-L)
- PMC
- PMC4828278
- OpenAlex
- W2294572602
- Cited by
- 73
- References
- 98
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 9 · 2023: 6 · 2022: 2 · 2021: 6 · 2020: 11 · 2019: 8 · 2018: 7 · 2017: 4 · 2016: 1
- FWCI
- 0.93
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Toxicon (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Allergy and Infectious Disease (AI103693, AI104993)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Vibrio bacteria research studies
- Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- Vibrio cholerae, zinc-dependent protease, cholera pathogenesis, intestinal mucosa, toxin regulation
- MeSH terms
- Amino Acid Sequence, Animals, Bacterial Proteins, Cholera, Humans, Intestinal Mucosa, Metalloendopeptidases, Thermolysin, Vibrio cholerae, Sequence Homology, Amino Acid, Models, Animal
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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