Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum

The lumen of the endoplasmic reticulum (ER) provides a unique folding envir onment that is distinct from other organelles supporting protein folding. T he relatively oxidizing milieu allows the formation of disulfide bonds. N-l inked oligosaccharides that are attached during synthesis play multiple rol es in the folding process of glycoproteins. They stabilize folded domains a nd increase protein solubility, which prevents aggregation of folding inter mediates. Glycans mediate the interaction of newly synthesized glycoprotein s with some resident ER folding factors, such as calnexin and calreticulin. Here we present an overview of the present knowledge on the folding proces s of the heavily glycosylated human immunodeficiency virus type 1 (HIV-1) e nvelope glycoprotein in the ER. (C) 2001 Societe francaise de biochimie et biologie moleculaire/Editions scientifiques et medicales Elsevier SAS. All rights reserved.