The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿
Vibrio tubiashii is a recently reemerging pathogen of larval bivalve mollusks, causing both toxigenic and invasive disease. Marine Vibrio spp. produce an array of extracellular products as potential pathogenicity factors. Culture supernatants of V. tubiashii have been shown to be toxic to oyster lar...
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ftpubmed:oai:pubmedcentral.nih.gov:2446533 2023-05-15T15:58:15+02:00 The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ Hasegawa, Hiroaki Lind, Erin J. Boin, Markus A. Häse, Claudia C. 2008-07 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446533 http://www.ncbi.nlm.nih.gov/pubmed/18456850 https://doi.org/10.1128/AEM.00061-08 en eng American Society for Microbiology (ASM) http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446533 http://www.ncbi.nlm.nih.gov/pubmed/18456850 http://dx.doi.org/10.1128/AEM.00061-08 Copyright © 2008, American Society for Microbiology Invertebrate Microbiology Text 2008 ftpubmed https://doi.org/10.1128/AEM.00061-08 2013-09-02T01:16:57Z Vibrio tubiashii is a recently reemerging pathogen of larval bivalve mollusks, causing both toxigenic and invasive disease. Marine Vibrio spp. produce an array of extracellular products as potential pathogenicity factors. Culture supernatants of V. tubiashii have been shown to be toxic to oyster larvae and were reported to contain a metalloprotease and a cytolysin/hemolysin. However, the structural genes responsible for these proteins have yet to be identified, and it is uncertain which extracellular products play a role in pathogenicity. We investigated the effects of the metalloprotease and hemolysin secreted by V. tubiashii on its ability to kill Pacific oyster (Crassostrea gigas) larvae. While V. tubiashii supernatants treated with metalloprotease inhibitors severely reduced the toxicity to oyster larvae, inhibition of the hemolytic activity did not affect larval toxicity. We identified structural genes of V. tubiashii encoding a metalloprotease (vtpA) and a hemolysin (vthA). Sequence analyses revealed that VtpA shared high homology with metalloproteases from a variety of Vibrio species, while VthA showed high homology only to the cytolysin/hemolysin of Vibrio vulnificus. Compared to the wild-type strain, a VtpA mutant of V. tubiashii not only produced reduced amounts of protease but also showed decreased toxicity to C. gigas larvae. Vibrio cholerae strains carrying the vtpA or vthA gene successfully secreted the heterologous protein. Culture supernatants of V. cholerae carrying vtpA but not vthA were highly toxic to Pacific oyster larvae. Together, these results suggest that the V. tubiashii extracellular metalloprotease is important in its pathogenicity to C. gigas larvae. Text Crassostrea gigas Pacific oyster PubMed Central (PMC) Pacific Applied and Environmental Microbiology 74 13 4101 4110 |
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English |
topic |
Invertebrate Microbiology |
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Invertebrate Microbiology Hasegawa, Hiroaki Lind, Erin J. Boin, Markus A. Häse, Claudia C. The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
topic_facet |
Invertebrate Microbiology |
description |
Vibrio tubiashii is a recently reemerging pathogen of larval bivalve mollusks, causing both toxigenic and invasive disease. Marine Vibrio spp. produce an array of extracellular products as potential pathogenicity factors. Culture supernatants of V. tubiashii have been shown to be toxic to oyster larvae and were reported to contain a metalloprotease and a cytolysin/hemolysin. However, the structural genes responsible for these proteins have yet to be identified, and it is uncertain which extracellular products play a role in pathogenicity. We investigated the effects of the metalloprotease and hemolysin secreted by V. tubiashii on its ability to kill Pacific oyster (Crassostrea gigas) larvae. While V. tubiashii supernatants treated with metalloprotease inhibitors severely reduced the toxicity to oyster larvae, inhibition of the hemolytic activity did not affect larval toxicity. We identified structural genes of V. tubiashii encoding a metalloprotease (vtpA) and a hemolysin (vthA). Sequence analyses revealed that VtpA shared high homology with metalloproteases from a variety of Vibrio species, while VthA showed high homology only to the cytolysin/hemolysin of Vibrio vulnificus. Compared to the wild-type strain, a VtpA mutant of V. tubiashii not only produced reduced amounts of protease but also showed decreased toxicity to C. gigas larvae. Vibrio cholerae strains carrying the vtpA or vthA gene successfully secreted the heterologous protein. Culture supernatants of V. cholerae carrying vtpA but not vthA were highly toxic to Pacific oyster larvae. Together, these results suggest that the V. tubiashii extracellular metalloprotease is important in its pathogenicity to C. gigas larvae. |
format |
Text |
author |
Hasegawa, Hiroaki Lind, Erin J. Boin, Markus A. Häse, Claudia C. |
author_facet |
Hasegawa, Hiroaki Lind, Erin J. Boin, Markus A. Häse, Claudia C. |
author_sort |
Hasegawa, Hiroaki |
title |
The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
title_short |
The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
title_full |
The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
title_fullStr |
The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
title_full_unstemmed |
The Extracellular Metalloprotease of Vibrio tubiashii Is a Major Virulence Factor for Pacific Oyster (Crassostrea gigas) Larvae▿ |
title_sort |
extracellular metalloprotease of vibrio tubiashii is a major virulence factor for pacific oyster (crassostrea gigas) larvae▿ |
publisher |
American Society for Microbiology (ASM) |
publishDate |
2008 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446533 http://www.ncbi.nlm.nih.gov/pubmed/18456850 https://doi.org/10.1128/AEM.00061-08 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2446533 http://www.ncbi.nlm.nih.gov/pubmed/18456850 http://dx.doi.org/10.1128/AEM.00061-08 |
op_rights |
Copyright © 2008, American Society for Microbiology |
op_doi |
https://doi.org/10.1128/AEM.00061-08 |
container_title |
Applied and Environmental Microbiology |
container_volume |
74 |
container_issue |
13 |
container_start_page |
4101 |
op_container_end_page |
4110 |
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1766393979241234432 |