Synthesis of Homo-oligomer Models, Functional Characterization, and Annotation of the Virulent HP33 Protein from the Vibrio harveyi Strain of Scale Drop and Muscle Necrosis Disease

Abstract

This study used a comprehensive bioinformatic application to discover the functions of the HP33 protein, which is responsible for the scale drop and muscle necrosis disease (SDMND) in fish. The main objective of the study was to the characterization of the HP33 protein and predict the homo-oligomer models to understand the physical effect of the protein for further research. At first, multiple sequence alignment and sub-cellular localization of the HP33 were predicted by the in-silico approach. The result suggests that this putative protein clustered with another hypothetical protein, Vibrio harveyi, and is an unstable, nonpolar, and outer membrane protein. Functional analysis of the protein by Pfam, InterProScan, and SMART tools predicts that the HP has a single functional domain that may signify a cluster of biosynthetic genes. The prediction of the active site, as well as the protein-protein interaction, were also predicted in this study. Furthermore, a protein-ligand docking investigation revealed two potential therapeutic compounds (Ferroheme C, Valine) that can be effective against HP33 pathogenesis. In conclusion, the homo-oligomers model's predictions and the ab-initio docking findings will offer important information for an additional immunological investigation, which may be beneficial in a future study on SDMND prophylaxis.