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.
Highlights
Vibrio parahaemolyticus is a marine-oriented pathogen, which can be detected in estuarine, coastal environments and seafood
Key Contribution: This study identified four fibrillar adhesin like proteins in V. parahaemolyticus, the structures and protein interfaces were emphasized to develop novel drugs for virulence inhibition
There were 64, 63, 33 and 42 Pfam (Ig-like fold domains, CL0159) hits identified in V. parahaemolyticus RIMD 2210633, V. parahaemolyticus CHN25, V. cholerae NCTC 9420 and Escherichia coli K-12 MG1655 genomes
Summary
Vibrio parahaemolyticus is a marine-oriented pathogen, which can be detected in estuarine, coastal environments and seafood. V. parahaemolyticus has resulted in significant economic loss in animal production and increased spread of foodborne diseases [1]. The intercellular communication and extracellular biofilm matrix development start with cell adhesion, which relies on the receptors located on cell surfaces. Among these receptors, the immunoglobulin-like [3] fold domains are the most widely distributed and typical class of proteins [4]. Ig-like domains play critical roles in Vibrio. VesB is a serine protease in Vibrio cholerae with an Ig-like fold domain at C-terminal of the protein; the deletion of the Ig-like domain resulted in the degradation of the protein [5]. The roles of Ig-like fold domains have been proposed to be related with stability, substrate specificity, cell surface association, and type II secretion of extracellular proteins [6].
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