Physicochemical Aspects of Open Reading Frame 4 of Hepatitis E Virus: A General Perspective

Abstract

Hepatitis E virus (HEV), a member of the family Hepeviridae, is the major cause of hepatitis E infections across the globe. Though the open reading frame 4 (ORF4) indispensability in the replication of HEV has been demonstrated, its physicochemical properties remain to be explored. Therefore, a thorough investigation of the physical and chemical properties of the ORF4 proteins, obtained from various HEV isolates, was carried out to examine their peculiar characteristics. The physicochemical properties considered for the present study included a number of charged amino acid residues, instability indices, aliphatic indices and grand average of hydropathy (GRAVY) scores. The comparative analyses predicted the basic, unstable, thermostable and hydrophobic nature of the ORF4 proteins. Delineation of various physicochemical components of ORF4 will assist in revealing specific patterns of these proteins, further which will increase our knowledge of HEV biology.