title: Structural principles controlling HIV envelope glycosylation.
abstract: 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.
authors.affiliation: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors.forename: Anna-Janina
authors.initials: AJ
authors.lastname: Behrens
authors.affiliation: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: max.crispin@bioch.ox.ac.uk.
authors.forename: Max
authors.initials: M
authors.lastname: Crispin
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D000939:Epitopes / Q000276:immunology; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism; D054299:env Gene Products, Human Immunodeficiency Virus / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism*
chemical_list: D000939:Epitopes; D011134:Polysaccharides; D054299:env Gene Products, Human Immunodeficiency Virus; D008358:Mannose