期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 44, 期 -, 页码 125-133出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2017.03.008
关键词
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资金
- Corpus Christi College, Oxford
- Scripps CHAVI-ID [1UM1AI100663]
- International AIDS Vaccine Initiative Neutralizing Antibody Center CAVD grant (Glycan characterization and Outer Domain glycoform design)
- European Union's Horizon Research and Innovation Programme [681137]
The heavily glycosylated, trimeric HIV-1 envelope (Env) protein is the sole viral protein exposed on the HIV-1 virion surface and is thus a main focus of antibody-mediated vaccine development. Dense glycosylation at the outer domain of Env constrains normal enzymatic processing, stalling the glycans at immature oligomannose-type structures. Furthermore, native trimerization imposes additional steric constraints, which generate an extensive 'trimer-induced mannose patch'. Importantly, the immature glycans present a highly conserved feature of the virus that is targeted by broadly neutralizing antibodies. Quantitative mass spectrometry of glycopeptides together with structures of the trimeric viral-spike define the steric principles controlling processing and provide a detailed map of the glycan shield.
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