Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function.
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.
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Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
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D001216:Asparagine / Q000235:genetics / Q000378:metabolism; D002459:Cell Fusion / Q000502:physiology; D002460:Cell Line; D006031:Glycosylation; D015700:HIV Envelope Protein gp41 / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D015497:HIV-1 / Q000235:genetics / Q000502:physiology*; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D011233:Precipitin Tests; D014779:Virus Replication / Q000235:genetics / Q000502:physiology
D015700:HIV Envelope Protein gp41; D001216:Asparagine