In Silico Approach Gives Insights into Ig-like Fold Containing Proteins in Vibrio parahaemolyticus: A Focus on the Fibrillar Adhesins

Abstract

Immunoglobulin-like (Ig-like) fold domains are abundant on the surface of bacteria, where they are required for cell-to-cell recognition, adhesion, biofilm formation, and conjugative transfer. Fibrillar adhesins are proteins with Ig-like fold(s) that have filamentous structures at the cell surface, being thinner and more flexible than pili. While the roles of fibrillar adhesins have been proposed in bacteria overall, their characterization in Vibrio parahaemolyticus has not been established and, therefore, understanding about fibrillar adhesins remain limited in V. parahaemolyticus. This in silico analysis can aid in the systematic identification of Ig-like-folded and fibrillar adhesin-like proteins in V. parahaemolyticus, opening new avenues for disease prevention by interfering in microbial interaction between V. parahaemolyticus and the host.

Genomic mining of Vibrio parahaemolyticus highlights prevalence of antimicrobial resistance genes and new genetic markers associated with AHPND and tdh + /trh + genotypes

“…Possibly, it is important in the protection against unfolding of the previously mentioned OmpA and other OMPs. The association with two immunoglobulin-like domain-containing proteins is seen, which are often surface proteins involved in cell-to-cell recognition, adhesion, biofilm formation, and conjugative transfer [ 56 , 57 ]. These domains are widely present in numerous proteins, and several have been identified in V. parahaemolyticus , such as adhesive factor VpadF [ 56 , 57 ].…”

“…The association with two immunoglobulin-like domain-containing proteins is seen, which are often surface proteins involved in cell-to-cell recognition, adhesion, biofilm formation, and conjugative transfer [ 56 , 57 ]. These domains are widely present in numerous proteins, and several have been identified in V. parahaemolyticus , such as adhesive factor VpadF [ 56 , 57 ]. Association with toxin gene ccdB indicated the importance of the toxin-antitoxin (TA) system ccdA-ccdB, consisting of the stable toxin ccdB and less stable antitoxin ccdA to neutralize the toxin.…”

Obacunone, a Promising Phytochemical Triterpenoid: Research Progress on Its Pharmacological Activity and Mechanism

“…In a computer simulation study, four novel fibrillar adhesin-like proteins, WP_005477759.1, WP_005480168.1, WP_005489282.1, and WP_005490731.1, were identified in Vibrio parahaemolyticus. A previous study analyzed the binding of 277 compounds to these four proteins and found that, except for the slightly weaker binding of WP_005480168.1, the binding of obacunone to the remaining three ranked in the top five, revealing its potential to inhibit the virulence of Vibrio parahaemolyticus on the host [64].…”