Comparative analysis of amino acid sequences from envelope proteins isolated from different hepatitis C virus variants: possible role of conservativeand variable regions

Sequences of the E1 and E2 envelope proteins of hepatitis C virus (HCV) (82 7 non-identical items) were collected from available sources and aligned. A nalysis of the alignment identified regions with different sequence variabi lity. It was found that 33% and 50% of positions within E1 and E2, respecti vely, were highly conservative. Such conservation can be considered as the minimum for maintaining stability of the three-dimensional structure and fu nction of these proteins. Conserved cysteines in E1 and E2 (eight and 18 re sidues, respectively) were presumed to form intramolecular disulphide bonds . Both envelope proteins were predicted to contain 14 conservative glycosyl ation sites. Two additional glycosylation sites were predicted in 58% of E1 and 30% of E2 sequences within the corresponding regions. We describe the positions of six conservative regions in E1 and E2, which have several char ged and aromatic residues known to participate frequently in protein-protei n recognition. Peculiarities in the amino acid content of conservative frag ments and putative differences in glycosylation were considered with regard to antigenic specificity and possible binding to surface structures of tar get cells. We also analysed the hypervariable region 1 (HVR1), located in t he E2 protein. Aligned positions of HVR1 were described in relation to the maintenance of conformational stability and recognition of cell receptors.