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Harnessing post-translational modifications for next-generation HIV immunogens

Harnessing post-translational modifications for next-generation HIV immunogens
Harnessing post-translational modifications for next-generation HIV immunogens

The extensive post-translational modifications of the envelope spikes of the human immunodeficiency virus (HIV) present considerable challenges and opportunities for HIV vaccine design. These oligomeric glycoproteins typically have over 30 disulfide bonds and around a 100 N-linked glycosylation sites, and are functionally dependent on protease cleavage within the secretory system. The resulting mature structure adopts a compact fold with the vast majority of its surface obscured by a protective shield of glycans which can be targeted by broadly neutralizing antibodies (bnAbs). Despite the notorious heterogeneity of glycosylation, rare B-cell lineages can evolve to utilize and cope with viral glycan diversity, and these structures therefore present promising targets for vaccine design. The latest generation of recombinant envelope spike mimetics contains re-engineered post-translational modifications to present stable antigens to guide the development of bnAbs by vaccination.

0300-5127
691-698
Allen, Joel D.
c873d886-2a66-475b-ae04-57a10b37e716
Sanders, Rogier W.
d3b67c2c-c725-42e7-b972-50b30be67c74
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Allen, Joel D.
c873d886-2a66-475b-ae04-57a10b37e716
Sanders, Rogier W.
d3b67c2c-c725-42e7-b972-50b30be67c74
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Allen, Joel D., Sanders, Rogier W., Doores, Katie J. and Crispin, Max (2018) Harnessing post-translational modifications for next-generation HIV immunogens. Biochemical Society Transactions, 46 (3), 691-698. (doi:10.1042/BST20170394).

Record type: Review

Abstract

The extensive post-translational modifications of the envelope spikes of the human immunodeficiency virus (HIV) present considerable challenges and opportunities for HIV vaccine design. These oligomeric glycoproteins typically have over 30 disulfide bonds and around a 100 N-linked glycosylation sites, and are functionally dependent on protease cleavage within the secretory system. The resulting mature structure adopts a compact fold with the vast majority of its surface obscured by a protective shield of glycans which can be targeted by broadly neutralizing antibodies (bnAbs). Despite the notorious heterogeneity of glycosylation, rare B-cell lineages can evolve to utilize and cope with viral glycan diversity, and these structures therefore present promising targets for vaccine design. The latest generation of recombinant envelope spike mimetics contains re-engineered post-translational modifications to present stable antigens to guide the development of bnAbs by vaccination.

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Allen_BiocSocTrans_2018_nihms-970701 - Accepted Manuscript
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Accepted/In Press date: 17 April 2018
e-pub ahead of print date: 21 May 2018

Identifiers

Local EPrints ID: 422838
URI: https://eprints.soton.ac.uk/id/eprint/422838
ISSN: 0300-5127
PURE UUID: 5b24b7c0-e478-497b-bb10-a716cc487274
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 06 Aug 2018 16:30
Last modified: 22 May 2019 04:01

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Contributors

Author: Joel D. Allen
Author: Rogier W. Sanders
Author: Katie J. Doores
Author: Max Crispin ORCID iD

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