Targeting glycans of HIV envelope glycoproteins for vaccine design

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).

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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Contributors

Author: Max Crispin

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