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

A Land, I Braakman

Journal: Biochimie 2001;83(8):783-90

PMID: 11530211

Full Text on Elsevier Science View on PubMed

Abstract

The lumen of the endoplasmic reticulum (ER) provides a unique folding environment that is distinct from other organelles supporting protein folding. The relatively oxidizing milieu allows the formation of disulfide bonds. N-linked oligosaccharides that are attached during synthesis play multiple roles in the folding process of glycoproteins. They stabilize folded domains and increase protein solubility, which prevents aggregation of folding intermediates. Glycans mediate the interaction of newly synthesized glycoproteins with some resident ER folding factors, such as calnexin and calreticulin. Here we present an overview of the present knowledge on the folding process of the heavily glycosylated human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein in the ER.

Address: Department of Bio-Organic Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
DOI: 10.1016/s0300-9084(01)01314-1

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MeSH Terms: Amino Acid Sequence, Calcium-Binding Proteins, Calnexin, Calreticulin, Carrier Proteins, Endoplasmic Reticulum, Endoplasmic Reticulum Chaperone BiP, Glycoproteins, Glycosylation, HIV Envelope Protein gp160, HIV-1, Heat-Shock Proteins, Humans, Molecular Chaperones, Molecular Sequence Data, Protein Disulfide-Isomerases, Protein Folding, Protein Sorting Signals, Ribonucleoproteins
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