Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens

Journal article

The envelope spike of HIV is one of the most highly N-glycosylated structures found in nature. However, despite extensive research revealing essential functional roles in infection and immune evasion, the chemical structures of the glycans on the native viral envelope glycoprotein gp120--as opposed to recombinantly generated gp120--have not been described. Here, we report on the identity of the N-linked glycans from primary isolates of HIV-1 (clades A, B, and C) and from the simian immunodefi...

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Authors: Doores, K; Bonomelli, C; Harvey, D; Vasiljevic, S; Dwek, R

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: National Academy of Sciences
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 107
• Issue: 31
• Pages: 13800-13805
• Publication date: 2010-08-01
• DOI: 10.1073/pnas.1006498107
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Polysaccharides; Antigens, Viral; HIV-1; Glycosylation; Cell Line; HIV Envelope Protein gp120; Oligosaccharides; Virion; Humans; Golgi Apparatus; Membrane Glycoproteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Simian immunodeficiency virus; Viral Envelope Proteins; Kinetics