Biological properties of recombinant HIV envelope synthesized in CHO glycosylation-mutant cell lines

Virology
E FenouilletR Drillien

Abstract

N-glycosylation of the human immunodeficiency virus type-1 envelope (Env) glycoprotein precursor (gp160) occurs by transfer of Glc3Man9GlcNAc2 onto the nascent protein. Maturation then occurs via cleavage of the three Glc residues, which starts during translation. These events are considered necessary to create Env functional conformation: treatment with "alpha"-glucosidase inhibitors, but not alpha-mannosidase inhibitors (i) impairs gp160 cleavage into gp120 and gp41, (ii) diminishes the accessibility of gp120 V3 region, (iii) prevents gp120 binding to its CD4 receptor, and (iv) prevents gp41-mediated membrane fusion. These inhibitors are of therapeutic interest. Here, using a collection of parent and mutant CHO cells that possess mutations in different steps of glycosylation, we reassessed the role of glycans in both the processing and the properties of recombinant gp160 expressed from a vaccinia virus vector. Mutant cells were as follows: Lec23 (which lacks alpha-glucosidase I activity) produces a collection of triglucosylated structures (Glc3Man7-9GlcNAc2); LEC10 (which has increased GlcNAc transferase III activity) produces complex glycans with a bisected GlcNAc residue; Lec1 (which lacks GlcNAc transferase I) and Lec3.2.8...Continue Reading

Citations

Jun 15, 2006·Amino Acids·E KarnaukhovaB Golding
Jun 25, 2005·Journal of Medical Virology·Sibusiso P NkosiMaria A Papathanasopoulos
Dec 1, 1998·The Journal of Peptide Research : Official Journal of the American Peptide Society·R BarboucheJ M Sabatier
Nov 21, 1997·Journal of Molecular Biology·N W DouglasR S Daniels

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