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Targeting glycans of HIV envelope glycoproteins for vaccine design

Targeting glycans of HIV envelope glycoproteins for vaccine design
Targeting glycans of HIV envelope glycoproteins for vaccine design
The surface of the envelope spike of the human immunodeficiency virus (HIV) is covered with a dense array of glycans, which is sufficient to impede the host antibody response while maintaining a window for receptor recognition. The glycan density significantly exceeds that typically observed on self glycoproteins and is sufficiently high to disrupt the maturation process of glycans, from oligomannose- to complex-type glycosylation, that normally occurs during glycoprotein transit through the secretory system. It is notable that this generates a degree of homogeneity not seen in the highly mutated protein moiety. The conserved, close glycan packing and divergences from default glycan processing give a window for immune recognition. Encouragingly, in a subset of individuals, broadly neutralizing antibodies (bNAbs) have been isolated that recognize these features and are protective in passive-transfer models. Here, we review the recent advances in our understanding of the glycan shield of HIV and outline the strategies that are being pursued to elicit glycan-binding bNAbs by vaccination.
Royal Society of Chemistry
Behrens, Anna Janina
ed584c40-79cb-4de9-bb9c-bd68c71d6a68
Seabright, Gemma E.
09e75998-09b0-465f-a059-c89b07f3b2c3
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Tan, Zhongping
Wang, Lai-Xi
Behrens, Anna Janina
ed584c40-79cb-4de9-bb9c-bd68c71d6a68
Seabright, Gemma E.
09e75998-09b0-465f-a059-c89b07f3b2c3
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Tan, Zhongping
Wang, Lai-Xi

Behrens, Anna Janina, Seabright, Gemma E. and Crispin, Max (2017) Targeting glycans of HIV envelope glycoproteins for vaccine design. In, Tan, Zhongping and Wang, Lai-Xi (eds.) Chemical Biology of Glycoproteins. London. Royal Society of Chemistry. (doi:10.1039/9781782623823-00300).

Record type: Book Section

Abstract

The surface of the envelope spike of the human immunodeficiency virus (HIV) is covered with a dense array of glycans, which is sufficient to impede the host antibody response while maintaining a window for receptor recognition. The glycan density significantly exceeds that typically observed on self glycoproteins and is sufficiently high to disrupt the maturation process of glycans, from oligomannose- to complex-type glycosylation, that normally occurs during glycoprotein transit through the secretory system. It is notable that this generates a degree of homogeneity not seen in the highly mutated protein moiety. The conserved, close glycan packing and divergences from default glycan processing give a window for immune recognition. Encouragingly, in a subset of individuals, broadly neutralizing antibodies (bNAbs) have been isolated that recognize these features and are protective in passive-transfer models. Here, we review the recent advances in our understanding of the glycan shield of HIV and outline the strategies that are being pursued to elicit glycan-binding bNAbs by vaccination.

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Published date: 27 March 2017

Identifiers

Local EPrints ID: 414495
URI: https://eprints.soton.ac.uk/id/eprint/414495
PURE UUID: 241b80dc-0701-4bdd-ab7a-60eead80f6ed
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 03 Oct 2017 16:31
Last modified: 14 Mar 2019 01:25

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