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

Maria Panico, Laura Bouché, Daniel Binet, Michael John O'Connor, Dinah Rahman, Poh Choo Pang, Kevin Canis, Simon J. North, Ronald Charles Desrosiers, Elena Chertova, Brandon F. Keele, Julian W. Bess, Jeffrey D. Lifson, Stuart M. Haslam, Anne Dell, Howard R. Morris

Research output: Contribution to journalArticle

35 Citations (Scopus)

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.

Original languageEnglish (US)
Article number32956
JournalScientific Reports
Volume6
DOIs
StatePublished - Sep 8 2016

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Neutralizing Antibodies
Glycosylation
Virion
HIV-1
Polysaccharides
Vaccines
Virus Attachment
AIDS Vaccines
Glycopeptides
Membrane Glycoproteins
Lymphocytes
Viruses
T-Lymphocytes
Antigens
Antibodies

ASJC Scopus subject areas

  • General

Cite this

Panico, M., Bouché, L., Binet, D., O'Connor, M. J., Rahman, D., Pang, P. C., ... Morris, H. R. (2016). Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding. Scientific Reports, 6, [32956]. https://doi.org/10.1038/srep32956

Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding. / Panico, Maria; Bouché, Laura; Binet, Daniel; O'Connor, Michael John; Rahman, Dinah; Pang, Poh Choo; Canis, Kevin; North, Simon J.; Desrosiers, Ronald Charles; Chertova, Elena; Keele, Brandon F.; Bess, Julian W.; Lifson, Jeffrey D.; Haslam, Stuart M.; Dell, Anne; Morris, Howard R.

In: Scientific Reports, Vol. 6, 32956, 08.09.2016.

Research output: Contribution to journalArticle

Panico, M, Bouché, L, Binet, D, O'Connor, MJ, Rahman, D, Pang, PC, Canis, K, North, SJ, Desrosiers, RC, Chertova, E, Keele, BF, Bess, JW, Lifson, JD, Haslam, SM, Dell, A & Morris, HR 2016, 'Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding', Scientific Reports, vol. 6, 32956. https://doi.org/10.1038/srep32956
Panico, Maria ; Bouché, Laura ; Binet, Daniel ; O'Connor, Michael John ; Rahman, Dinah ; Pang, Poh Choo ; Canis, Kevin ; North, Simon J. ; Desrosiers, Ronald Charles ; Chertova, Elena ; Keele, Brandon F. ; Bess, Julian W. ; Lifson, Jeffrey D. ; Haslam, Stuart M. ; Dell, Anne ; Morris, Howard R. / Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding. In: Scientific Reports. 2016 ; Vol. 6.
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