A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization
Open Access
- 6 February 2013
- journal article
- Published by Springer Nature in Retrovirology
- Vol. 10 (1) , 14
- https://doi.org/10.1186/1742-4690-10-14
Abstract
Glycans on the human immunodeficiency virus (HIV) envelope glycoprotein (Env) play an important role in viral infection and evasion of neutralization by antibodies. In this study, all 25 potential N-linked glycosylation sites (PNGS) on the HIV-1 CRF07_BC Env, FE, were mutated individually to study the effect of their removal on viral infectivity, virion production, and antibody-mediated neutralization.Keywords
This publication has 72 references indexed in Scilit:
- The Highly Conserved Glycan at Asparagine 260 of HIV-1 gp120 Is Indispensable for Viral EntryJournal of Biological Chemistry, 2011
- Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9Nature, 2011
- Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formationVaccine, 2011
- Trimeric HIV-1 glycoprotein gp140 immunogens and native HIV-1 envelope glycoproteins display the same closed and open quaternary molecular architecturesProceedings of the National Academy of Sciences, 2011
- Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobilityProceedings of the National Academy of Sciences, 2009
- Glycosylation Site-Specific Analysis of Clade C HIV-1 Envelope ProteinsJournal of Proteome Research, 2009
- Role of the HIV gp120 Conserved Domain 1 in Processing and Viral EntryJournal of Biological Chemistry, 2008
- Molecular architecture of native HIV-1 gp120 trimersNature, 2008
- A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodiesProceedings of the National Academy of Sciences, 2008
- Structural definition of a conserved neutralization epitope on HIV-1 gp120Nature, 2007