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

• Main Authors: Fabián Galvis (Author), Juan L. Barja (Author), Manuel L. Lemos (Author), Miguel Balado (Author)
• Format: Book
• Published: MDPI AG, 2021-04-01T00:00:00Z.
• Subjects: article
• Online Access: Connect to this object online.

Summary

<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>.

Item Description

10.3390/antibiotics10040391
2079-6382