Elucidating Structural, Functional and Phylogenetic Relationship of Large Envelope Protein of Hepatitis B V irus

Abstract

Objectives: To predict the structure of L-HBsAg envelope protein of Hepatitis B Virus and its evolutionary relationship. Methods: Bioinformatics Computational methods were used for the structure prediction and evolutionary conservation analysis of large envelope protein of Hepatitis B virus (L-HBsAg). Structure prediction L-HBsAg envelope protein was done using Multi-template homology modeling method using Schrodinger software. Phylogenetic tree was constructed by MEGA tool to identify protein similarity of L-HBsAg protein with other genotypes of HBV. Findings: Modelled structure of L-HBsAg protein shows that this protein has single alpha-helix and loop structure. Multiple sequence alignment result shows that L-HBsAg belongs to family of vMSA (pfam00695, major surface antigen from hepadnavirus) conserved domain. Phylogenetic tree reveals that L-HBsAg shows similarity with other proteins of HBV protein like preS protein and envelope protein. Novelty: Structural analysis identifies the binding properties of L-HBsAg protein. This study concluded that large envelope protein of HBV can be potent drug target for designing a novel drug. Keywords: LHBsAg; HBV; evolutionary analysis; structure prediction; dane particles