Computer predictions of functional, topogenic, and antigenic domains in human immunodeficiency virus-2 envelope glycoprotein.

The gp160 of HIV-2 was studied with the aid of computer programs that provide the hydrophilicity, surface probability, flexibility, and antigenicity index of the amino-acid sequence in a polypeptide chain. Such analyses allow the identification of hydrophobic amino-acid domains in the polypeptide chain that may serve as putative proteolytic cleavage signals and putative antigenic domains. It was possible to define the function of hydrophobic domains in the polypeptide chain that serve as signals and amino-acid sequences involved in the transfer of the polypeptide through the cellular membrane by the cellular signal recognition protein (SRP) complex. By comparison to reported properties of HIV-1 gp160 and SIVMAC gp160, it was possible to define antigenic domains in the loops of gp120 resulting from the reported interchain disulfide bonds defining putative antigenic domains specific for HIV-2.