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- Publisher Website: 10.1111/jfd.13120
- Scopus: eid_2-s2.0-85075733607
- PMID: 31779054
- WOS: WOS:000507925200011
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Article: Outer membrane protein A (OmpA) is a potential virulence factor of Vibrio alginolyticus strains isolated from diseased fish
Title | Outer membrane protein A (OmpA) is a potential virulence factor of Vibrio alginolyticus strains isolated from diseased fish |
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Authors | |
Keywords | Galleria mellonella MALDI‐TOF mass spectrometry ompA two‐dimensional gel electrophoresis Vibrio alginolyticus |
Issue Date | 2020 |
Publisher | Wiley-Blackwell Publishing Ltd. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2761 |
Citation | Journal of Fish Diseases, 2020, v. 43 n. 2, p. 275-284 How to Cite? |
Abstract | Vibrio alginolyticus is one of the most serious causative agents of diseases in cultured marine fish and shellfish. However, the characteristics of virulence factors in pathogenic V. alginolyticus are poorly known. To gain insight into fish diseases caused by V. alginolyticus, we carried out two‐dimensional gel electrophoresis (2‐DE) combined with MALDI‐TOF mass spectrometry to identify uniquely expressed proteins in the disease‐causing V. alginolyticus. V. alginolyticus strains were isolated from marine environments and diseased fish obtained from southern Thailand. We identified seven unique proteins in the disease‐causing V. alginolyticus strain. Among those, the outer membrane protein A (OmpA) had the strongest expression. Therefore, the function of this protein was further analysed. To investigate the role of OmpA protein, an in‐frame deletion mutant of ompA was constructed using the homologous recombination method. Although the ompA mutant V. alginolyticus strain (ΔompA) grew normally, the mutant exhibited a significant defect in the swarming ability and the biofilm formation. Furthermore, Galleria mellonella larvae injected with the mutant bacteria had a significantly greater survival percentage than those injected with the wild‐type strain, demonstrating that OmpA protein is required for the pathogenicity of V. alginolyticus. Together, this study suggests a potential target for vaccine development against pathogenic V. alginolyticus strain. |
Description | link_to_subscribed_fulltext |
Persistent Identifier | http://hdl.handle.net/10722/294624 |
ISSN | 2023 Impact Factor: 2.2 2023 SCImago Journal Rankings: 0.656 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Bunpa, S | - |
dc.contributor.author | Chaichana, N | - |
dc.contributor.author | Teng, JLL | - |
dc.contributor.author | LEE, HH | - |
dc.contributor.author | Woo, PCY | - |
dc.contributor.author | Sermwittayawong, D | - |
dc.contributor.author | Sawangjaroen, N | - |
dc.contributor.author | Sermwittayawong, N | - |
dc.date.accessioned | 2020-12-08T07:39:36Z | - |
dc.date.available | 2020-12-08T07:39:36Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Journal of Fish Diseases, 2020, v. 43 n. 2, p. 275-284 | - |
dc.identifier.issn | 0140-7775 | - |
dc.identifier.uri | http://hdl.handle.net/10722/294624 | - |
dc.description | link_to_subscribed_fulltext | - |
dc.description.abstract | Vibrio alginolyticus is one of the most serious causative agents of diseases in cultured marine fish and shellfish. However, the characteristics of virulence factors in pathogenic V. alginolyticus are poorly known. To gain insight into fish diseases caused by V. alginolyticus, we carried out two‐dimensional gel electrophoresis (2‐DE) combined with MALDI‐TOF mass spectrometry to identify uniquely expressed proteins in the disease‐causing V. alginolyticus. V. alginolyticus strains were isolated from marine environments and diseased fish obtained from southern Thailand. We identified seven unique proteins in the disease‐causing V. alginolyticus strain. Among those, the outer membrane protein A (OmpA) had the strongest expression. Therefore, the function of this protein was further analysed. To investigate the role of OmpA protein, an in‐frame deletion mutant of ompA was constructed using the homologous recombination method. Although the ompA mutant V. alginolyticus strain (ΔompA) grew normally, the mutant exhibited a significant defect in the swarming ability and the biofilm formation. Furthermore, Galleria mellonella larvae injected with the mutant bacteria had a significantly greater survival percentage than those injected with the wild‐type strain, demonstrating that OmpA protein is required for the pathogenicity of V. alginolyticus. Together, this study suggests a potential target for vaccine development against pathogenic V. alginolyticus strain. | - |
dc.language | eng | - |
dc.publisher | Wiley-Blackwell Publishing Ltd. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2761 | - |
dc.relation.ispartof | Journal of Fish Diseases | - |
dc.rights | Submitted (preprint) Version This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. Accepted (peer-reviewed) Version This is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. | - |
dc.subject | Galleria mellonella | - |
dc.subject | MALDI‐TOF mass spectrometry | - |
dc.subject | ompA | - |
dc.subject | two‐dimensional gel electrophoresis | - |
dc.subject | Vibrio alginolyticus | - |
dc.title | Outer membrane protein A (OmpA) is a potential virulence factor of Vibrio alginolyticus strains isolated from diseased fish | - |
dc.type | Article | - |
dc.identifier.email | Teng, JLL: llteng@hku.hk | - |
dc.identifier.email | Woo, PCY: pcywoo@hkucc.hku.hk | - |
dc.identifier.authority | Teng, JLL=rp00277 | - |
dc.identifier.authority | Woo, PCY=rp00430 | - |
dc.identifier.doi | 10.1111/jfd.13120 | - |
dc.identifier.pmid | 31779054 | - |
dc.identifier.scopus | eid_2-s2.0-85075733607 | - |
dc.identifier.hkuros | 320420 | - |
dc.identifier.volume | 43 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 275 | - |
dc.identifier.epage | 284 | - |
dc.identifier.isi | WOS:000507925200011 | - |
dc.publisher.place | United Kingdom | - |