| Summary: | 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 <i>Vibrio parahaemolyticus</i> has not been established and, therefore, understanding about fibrillar adhesins remain limited in <i>V</i><i>. parahaemolyticus</i>. This in silico analysis can aid in the systematic identification of Ig-like-folded and fibrillar adhesin-like proteins in <i>V. parahaemolyticus</i>, opening new avenues for disease prevention by interfering in microbial interaction between <i>V. parahaemolyticus</i> and the host.
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