Domain Organization of Lentiviral and Betaretroviral Surface Envelope Glycoproteins Modeled with AlphaFold.

ABSTRACT: The surface envelope glycoproteins of nonprimate lentiviruses and betaretroviruses share sequence similarity with the inner proximal domain β-sandwich of the human immunodeficiency virus type 1 (HIV-1) gp120 glycoprotein that faces the transmembrane glycoprotein as well as patterns of cysteine and glycosylation site distribution that points to a similar two-domain organization in at least some lentiviruses. Here, high-reliability models of the surface glycoproteins obtained with the AlphaFold algorithm are presented for the gp135 glycoprotein of the small ruminant caprine arthritis-encephalitis (CAEV) and visna lentiviruses and the betaretroviruses Jaagsiekte sheep retrovirus (JSRV), mouse mammary tumor virus (MMTV), and consensus human endogenous retrovirus type K (HERV-K). The models con

SUBMITTER: Hotzel I 

PROVIDER: S-EPMC8791290 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature