Chemical Biology of Glycoproteins
CHAPTER 11: Targeting Glycans of HIV Envelope Glycoproteins for Vaccine Design
Published:20 Mar 2017
Special Collection: 2017 ebook collectionSeries: Chemical Biology
A. Behrens, G. E. Seabright, and M. Crispin, in Chemical Biology of Glycoproteins, ed. Z. Tan and L. Wang, The Royal Society of Chemistry, 2017, pp. 300-357.
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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.