PLoS ONE · 2011 · 233 citations · 40 references
The N-linked oligomannose glycans of HIV gp120 are a target for both microbicide and vaccine design. The extent of cross-clade conservation of HIV oligomannose glycans is therefore a critical consideration for the development of HIV prophylaxes. We measured the oligomannose content of virion-associated gp120 from primary virus from PBMCs for a range of viral isolates and showed cross-clade elevation (62-79%) of these glycans relative to recombinant, monomeric gp120 (∼30%). We also confirmed that pseudoviral production systems can give rise to notably elevated gp120 oligomannose levels (∼98%), compared to gp120 derived from a single-plasmid viral system using the HIV(LAI) backbone (56%). This study highlights differences in glycosylation between virion-associated and recombinant gp120.
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Antibody neutralization and escape by HIV-1
Xiping Wei, Julie M. Decker, Shuyi Wang et al. · Nature · 2003 · 2.4K citations
Ming Li, Feng Gao, John R. Mascola et al. · Journal of Virology · 2005 · 1.1K citations · Full text
Vaccine-elicited Neutralizing Antibodies, Standardized Assessments, Immunodeficiencies +17
HIV vaccine design and the neutralizing antibody problem
Dennis R. Burton, Ronald C. Desrosiers, Robert W. Doms et al. · Nature Immunology · 2004 · 764 citations