ArticleArchives of virology1992
An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus.
Article in Archives of virology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 49 citations in OpenAlex.
- Serum glycan-binding IgG antibodies in HIV-1 infection and during the development of broadly neutralizing responses.AIDS (London, England) · 2017Article
- The HIV glycan shield as a target for broadly neutralizing antibodies.The FEBS journal · 2015Review
- Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate.PloS one · 2015Article
- High-throughput profiling of anti-glycan humoral responses to SIV vaccination and challenge.PloS one · 2013Article
- Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.Immunological reviews · 2012Review
- Solution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120.Journal of virology · 2012Article
- Candidate antibody-based therapeutics against HIV-1.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2012Review
- Simian immunodeficiency virus from the sooty mangabey and rhesus macaque is modified with O-linked carbohydrate.Journal of virology · 2011Article
- Removal of a single N-linked glycan in human immunodeficiency virus type 1 gp120 results in an enhanced ability to induce neutralizing antibody responses.Journal of virology · 2008Article
- Location-specific, unequal contribution of the N glycans in simian immunodeficiency virus gp120 to viral infectivity and removal of multiple glycans without disturbing infectivity.Journal of virology · 1998Article
- NetOglyc: prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility.Glycoconjugate journal · 1998Article
- Peptide mimotopes of carbohydrate antigens.Immunologic research · 1998Review
- Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein.Journal of virology · 1996Article
- Sensitivity of HIV-1 to neutralization by antibodies against O-linked carbohydrate epitopes despite deletion of O-glycosylation signals in the V3 loop.Archives of virology · 1996Article
- Sequence diversity of V1 and V2 domains of gp120 from human immunodeficiency virus type 1: lack of correlation with viral phenotype.Journal of virology · 1995Article
- Immunological evidence for interactions between the first, second, and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1.Journal of virology · 1994Article
- Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies.Journal of virology · 1994Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies have disagreed about the presence of O-linked carbohydrate epitopes on gp 120 of HIV, although antibodies against short-chain O-linked glycans neutralize HIV infection and block syncytium formation in vitro. To settle this question, we analysed the O-linked glycans of gp 120 by chemical methods using purified HIV-1 gp 120 from cells infected with recombinant vaccinia virus solely expressing gp 160 or gp 120. Alkaline borohydride degradation of recombinant gp 120 released monosaccharides and also slightly larger structures (di/trisaccharides) by a beta-elimination, confirming the presence of simple O-linked oligosaccharides. The functional activity as neutralisation epitopes of the O-linked oligosaccharides expressed on recombinant gp 120 was preserved, since fusion between uninfected CD4+ cells and cells infected with recombinant vaccinia was blocked by monoclonal antibodies to the O-linked oligosaccharides of gp 120. Although the mechanism for HIV induction of O-linked oligosaccharide neoantigens is unknown, these results indicate that the O-linked neutralization epitopes are inherent to the glycoprotein itself, and that the unusual appearance of simple O-linked oligosaccharides on gp 120 is independent of any interaction between the host cell and retroviral genes other than env.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.