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Protein and glycan mimicry in HIV vaccine design

Protein and glycan mimicry in HIV vaccine design
Protein and glycan mimicry in HIV vaccine design
ntigenic mimicry is a fundamental tenet of structure-based vaccinology. Vaccine strategies for the human immunodeficiency virus type 1 (HIV-1) focus on the mimicry of its envelope spike (Env) due to its exposed location on the viral membrane and role in mediating infection. However, the virus has evolved to minimise the immunogenicity of conserved epitopes on the envelope spike. This principle is starkly illustrated by the presence of an extensive array of host-derived glycans which act to shield the underlying protein from antibody recognition. Despite these hurdles, a subset of HIV-infected individuals eventually develop broadly neutralising antibodies that recognise these virally-presented glycans. Effective HIV-1 immunogens are therefore likely to involve some degree of mimicry of both the protein and glycan components of Env. As such, considerable efforts have been made to characterise the structure of the envelope spike and its glycan shield. This review summarises the recent progress made in this field, with an emphasis on our growing understanding of the factors shaping the glycan shield of Env derived from both virus and soluble immunogens. We argue that recombinant mimics of the envelope spike are currently capable of capturing many features of the native viral glycan shield. Finally, we explore strategies through which the immunogenicity of Env glycans may be enhanced in the development of future immunogens.
0022-2836
Seabright, Gemma
fad04a63-47ad-4cdd-8cf7-eeecbc5060c0
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Burton, Dennis R.
a628ce77-b694-4e3c-86a5-11f4e20e1c7c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Seabright, Gemma
fad04a63-47ad-4cdd-8cf7-eeecbc5060c0
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Burton, Dennis R.
a628ce77-b694-4e3c-86a5-11f4e20e1c7c
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Seabright, Gemma, Doores, Katie J., Burton, Dennis R. and Crispin, Max (2019) Protein and glycan mimicry in HIV vaccine design. Journal of Molecular Biology. (doi:10.1016/j.jmb.2019.04.016).

Record type: Review

Abstract

ntigenic mimicry is a fundamental tenet of structure-based vaccinology. Vaccine strategies for the human immunodeficiency virus type 1 (HIV-1) focus on the mimicry of its envelope spike (Env) due to its exposed location on the viral membrane and role in mediating infection. However, the virus has evolved to minimise the immunogenicity of conserved epitopes on the envelope spike. This principle is starkly illustrated by the presence of an extensive array of host-derived glycans which act to shield the underlying protein from antibody recognition. Despite these hurdles, a subset of HIV-infected individuals eventually develop broadly neutralising antibodies that recognise these virally-presented glycans. Effective HIV-1 immunogens are therefore likely to involve some degree of mimicry of both the protein and glycan components of Env. As such, considerable efforts have been made to characterise the structure of the envelope spike and its glycan shield. This review summarises the recent progress made in this field, with an emphasis on our growing understanding of the factors shaping the glycan shield of Env derived from both virus and soluble immunogens. We argue that recombinant mimics of the envelope spike are currently capable of capturing many features of the native viral glycan shield. Finally, we explore strategies through which the immunogenicity of Env glycans may be enhanced in the development of future immunogens.

Text
Seabright et al_Manuscript with figures_corrections_unmarked - Accepted Manuscript
Available under License Creative Commons Attribution.
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More information

Accepted/In Press date: 13 April 2019
e-pub ahead of print date: 24 April 2019

Identifiers

Local EPrints ID: 430318
URI: http://eprints.soton.ac.uk/id/eprint/430318
ISSN: 0022-2836
PURE UUID: aff07ecb-2b18-4ed6-9817-feae4f4ece16
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 25 Apr 2019 16:30
Last modified: 26 Nov 2021 03:11

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Contributors

Author: Gemma Seabright
Author: Katie J. Doores
Author: Dennis R. Burton
Author: Max Crispin ORCID iD

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