The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>

<i>Vibrio neptunius</i> is an important pathogen of bivalve mollusks worldwide. Several metalloproteases have been described as virulence factors in species of <i>Vibrio</i> that are pathogenic to bivalves, but little is known about the contribution of these potential virulen...

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Main Authors: Fabián Galvis, Juan L. Barja, Manuel L. Lemos, Miguel Balado
Format: Article
Language:English
Published: MDPI AG 2021-04-01
Series:Antibiotics
Subjects:
Online Access:https://www.mdpi.com/2079-6382/10/4/391
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author Fabián Galvis
Juan L. Barja
Manuel L. Lemos
Miguel Balado
author_facet Fabián Galvis
Juan L. Barja
Manuel L. Lemos
Miguel Balado
author_sort Fabián Galvis
collection DOAJ
description <i>Vibrio neptunius</i> is an important pathogen of bivalve mollusks worldwide. Several metalloproteases have been described as virulence factors in species of <i>Vibrio</i> that are pathogenic to bivalves, but little is known about the contribution of these potential virulence factors to <i>Vibrio neptunius</i> pathogenesis. In silico analysis of the genome of <i>V. neptunius</i> strain PP-145.98 led to the identification of two hitherto uncharacterized chromosomal loci encoding a probable vibriolysin-like metalloprotease and a putative collagenase, which were designated VnpA and ColA, respectively. Single defective mutants of each gene were obtained in <i>V. neptunius</i> PP-145.98, and the phospholipase, esterase and collagenase activities were studied and compared with those of the wild-type strain. The results showed that the single inactivation of <i>vnpA</i> resulted in a 3-fold reduction in phospholipase/esterase activity. Inactivation of <i>colA</i> reduced the collagenase activity by 50%. Finally, infection challenges performed in oyster larvae showed that Δ<i>vnpA</i> and Δ<i>colA</i>—single mutant strains of <i>V. neptunius</i>—are between 2–3-fold less virulent than the wild-type strain. Thus, the present work demonstrates that the production of both VnpA and ColA is required for the full virulence of the bivalve pathogen <i>V. neptunius</i>.
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spelling doaj.art-abd97d92ff74434eb034100d105e049c2023-11-21T14:21:09ZengMDPI AGAntibiotics2079-63822021-04-0110439110.3390/antibiotics10040391The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>Fabián Galvis0Juan L. Barja1Manuel L. Lemos2Miguel Balado3Departamento de Microbiología y Parasitología, Instituto de Acuicultura y CIBUS-Facultad de Biología, Universidade de Santiago de Compostela, 15705 Santiago de Compostela, A Coruña, SpainDepartamento de Microbiología y Parasitología, Instituto de Acuicultura y CIBUS-Facultad de Biología, Universidade de Santiago de Compostela, 15705 Santiago de Compostela, A Coruña, SpainDepartamento de Microbiología y Parasitología, Instituto de Acuicultura y CIBUS-Facultad de Biología, Universidade de Santiago de Compostela, 15705 Santiago de Compostela, A Coruña, SpainDepartamento de Microbiología y Parasitología, Instituto de Acuicultura y CIBUS-Facultad de Biología, Universidade de Santiago de Compostela, 15705 Santiago de Compostela, A Coruña, Spain<i>Vibrio neptunius</i> is an important pathogen of bivalve mollusks worldwide. Several metalloproteases have been described as virulence factors in species of <i>Vibrio</i> that are pathogenic to bivalves, but little is known about the contribution of these potential virulence factors to <i>Vibrio neptunius</i> pathogenesis. In silico analysis of the genome of <i>V. neptunius</i> strain PP-145.98 led to the identification of two hitherto uncharacterized chromosomal loci encoding a probable vibriolysin-like metalloprotease and a putative collagenase, which were designated VnpA and ColA, respectively. Single defective mutants of each gene were obtained in <i>V. neptunius</i> PP-145.98, and the phospholipase, esterase and collagenase activities were studied and compared with those of the wild-type strain. The results showed that the single inactivation of <i>vnpA</i> resulted in a 3-fold reduction in phospholipase/esterase activity. Inactivation of <i>colA</i> reduced the collagenase activity by 50%. Finally, infection challenges performed in oyster larvae showed that Δ<i>vnpA</i> and Δ<i>colA</i>—single mutant strains of <i>V. neptunius</i>—are between 2–3-fold less virulent than the wild-type strain. Thus, the present work demonstrates that the production of both VnpA and ColA is required for the full virulence of the bivalve pathogen <i>V. neptunius</i>.https://www.mdpi.com/2079-6382/10/4/391<i>Vibrio neptunius</i>virulencebivalve mollusk pathogenmetalloproteasecollagenaseVnpA
spellingShingle Fabián Galvis
Juan L. Barja
Manuel L. Lemos
Miguel Balado
The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
Antibiotics
<i>Vibrio neptunius</i>
virulence
bivalve mollusk pathogen
metalloprotease
collagenase
VnpA
title The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
title_full The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
title_fullStr The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
title_full_unstemmed The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
title_short The Vibriolysin-Like Protease VnpA and the Collagenase ColA Are Required for Full Virulence of the Bivalve Mollusks Pathogen <i>Vibrio neptunius</i>
title_sort vibriolysin like protease vnpa and the collagenase cola are required for full virulence of the bivalve mollusks pathogen i vibrio neptunius i
topic <i>Vibrio neptunius</i>
virulence
bivalve mollusk pathogen
metalloprotease
collagenase
VnpA
url https://www.mdpi.com/2079-6382/10/4/391
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