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Structural principles controlling HIV envelope glycosylation

Structural principles controlling HIV envelope glycosylation
Structural principles controlling HIV envelope glycosylation

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.

0959-440X
125-133
Behrens, Anna Janina
ed584c40-79cb-4de9-bb9c-bd68c71d6a68
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Behrens, Anna Janina
ed584c40-79cb-4de9-bb9c-bd68c71d6a68
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Behrens, Anna Janina and Crispin, Max (2017) Structural principles controlling HIV envelope glycosylation. Current Opinion in Structural Biology, 44, 125-133. (doi:10.1016/j.sbi.2017.03.008).

Record type: Review

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.

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More information

e-pub ahead of print date: 29 March 2017
Published date: 1 June 2017

Identifiers

Local EPrints ID: 414335
URI: https://eprints.soton.ac.uk/id/eprint/414335
ISSN: 0959-440X
PURE UUID: 22a47e7f-0b45-4cd2-84da-5b0b892a8779
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 26 Sep 2017 16:30
Last modified: 14 Mar 2019 01:25

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Contributors

Author: Anna Janina Behrens
Author: Max Crispin ORCID iD

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