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Sci Rep. 2016 Sep 8;6:32956. doi: 10.1038/srep32956.

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding.

Author information

1
Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW7 2AZ, UK.
2
BioPharmaSpec, Suite 3.1 Lido Medical Centre, St. Saviours Road, Jersey, JE2 7LA, UK.
3
Department of Pathology, University of Miami, Miami, Florida, 33136, USA.
4
AIDS and Cancer Virus Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, Maryland 21702, USA.

Abstract

The surface envelope glycoprotein (SU) of Human immunodeficiency virus type 1 (HIV-1), gp120(SU) plays an essential role in virus binding to target CD4+ T-cells and is a major vaccine target. Gp120 has remarkably high levels of N-linked glycosylation and there is considerable evidence that this "glycan shield" can help protect the virus from antibody-mediated neutralization. In recent years, however, it has become clear that gp120 glycosylation can also be included in the targets of recognition by some of the most potent broadly neutralizing antibodies. Knowing the site-specific glycosylation of gp120 can facilitate the rational design of glycopeptide antigens for HIV vaccine development. While most prior studies have focused on glycan analysis of recombinant forms of gp120, here we report the first systematic glycosylation site analysis of gp120 derived from virions produced by infected T lymphoid cells and show that a single site is exclusively substituted with complex glycans. These results should help guide the design of vaccine immunogens.

PMID:
27604319
PMCID:
PMC5015092
DOI:
10.1038/srep32956
[Indexed for MEDLINE]
Free PMC Article

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