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Structure and immune recognition of the HIV glycan shield

Structure and immune recognition of the HIV glycan shield
Structure and immune recognition of the HIV glycan shield
Vaccine design efforts against the human immunodeficiency virus (HIV)
have been greatly stimulated by the observation that many infected patients eventually develop highly potent broadly neutralizing antibodies (bnAbs).
Importantly, these bnAbs have evolved to recognize not only the two protein components of the viral envelope protein (Env) but also the numerous glycans that form a protective barrier on the Env protein. Because Env is heavily glycosylated compared to host glycoproteins, the glycans have be- come targets for the antibody response. Therefore, considerable efforts have been made in developing and validating biophysical methods to elucidate the complex structure of the Env-spike glycoprotein, with its combination of glycan and protein epitopes. We illustrate here how the application of robust biophysical methods have transformed our understanding of the structure and function of the HIV Env spike and stimulated innovation in vaccine design strategies that takes into account the essential glycan components.
1936-122X
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Ward, Andrew B.
7b743524-72d4-448d-b645-11c55782b656
Wilson, Ian A.
af4c8f24-9401-451d-b7d7-7f25cc80182f
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Ward, Andrew B.
7b743524-72d4-448d-b645-11c55782b656
Wilson, Ian A.
af4c8f24-9401-451d-b7d7-7f25cc80182f

Crispin, Max, Ward, Andrew B. and Wilson, Ian A. (2018) Structure and immune recognition of the HIV glycan shield. Annual Review of Biophysics. (doi:10.1146/annurev-biophys-060414-034156).

Record type: Review

Abstract

Vaccine design efforts against the human immunodeficiency virus (HIV)
have been greatly stimulated by the observation that many infected patients eventually develop highly potent broadly neutralizing antibodies (bnAbs).
Importantly, these bnAbs have evolved to recognize not only the two protein components of the viral envelope protein (Env) but also the numerous glycans that form a protective barrier on the Env protein. Because Env is heavily glycosylated compared to host glycoproteins, the glycans have be- come targets for the antibody response. Therefore, considerable efforts have been made in developing and validating biophysical methods to elucidate the complex structure of the Env-spike glycoprotein, with its combination of glycan and protein epitopes. We illustrate here how the application of robust biophysical methods have transformed our understanding of the structure and function of the HIV Env spike and stimulated innovation in vaccine design strategies that takes into account the essential glycan components.

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e-pub ahead of print date: 29 March 2018

Identifiers

Local EPrints ID: 420747
URI: http://eprints.soton.ac.uk/id/eprint/420747
ISSN: 1936-122X
PURE UUID: 9999079b-909a-4c3d-b509-7753e5f533c0
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 14 May 2018 16:30
Last modified: 22 Nov 2021 03:16

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Contributors

Author: Max Crispin ORCID iD
Author: Andrew B. Ward
Author: Ian A. Wilson

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