Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function

Douglas A. Dedera, Ruili Gu, Lee Ratner

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

Transmembrane envelope protein (TM) residues 100, 105, and 128 of human immunodeficiency virus type 1 (HIV-1) strain HXB2 are potential sites for asparagine-linked oligosaccharide additions which are conserved among HIV-1 isolates, and all other lentivirus TM proteins. Site-specific mutants of each of the asparagine residues did not eliminate the ability of the virus to infect and replicate in CD4+ cells, but infectivity was reduced with all of these mutants, and syncytia induction was attenuated with two of these mutants. Studies of envelope expression of the mutant with the most severe defect demonstrated no significant effects on envelope protein synthesis, conformation, processing, multimerization, or release into the culture medium, suggesting that N-linked oligosaccharides are important in the specific fusion activity of TM.

Original languageEnglish
Pages (from-to)377-382
Number of pages6
JournalVirology
Volume187
Issue number1
DOIs
StatePublished - Mar 1992

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