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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-4
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pubmed:dateCreated |
1992-10-14
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Tumor-Associated...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tn antigen
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pubmed:status |
MEDLINE
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pubmed:issn |
0304-8608
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
126
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pubmed:geneSymbol |
env
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1381907-Animals,
pubmed-meshheading:1381907-Antibodies, Monoclonal,
pubmed-meshheading:1381907-Antigens, Neoplasm,
pubmed-meshheading:1381907-Antigens, Tumor-Associated, Carbohydrate,
pubmed-meshheading:1381907-Antigens, Viral,
pubmed-meshheading:1381907-Cell Fusion,
pubmed-meshheading:1381907-Cell Line,
pubmed-meshheading:1381907-Chromatography, Gel,
pubmed-meshheading:1381907-Epitopes,
pubmed-meshheading:1381907-Genes, env,
pubmed-meshheading:1381907-HIV Envelope Protein gp120,
pubmed-meshheading:1381907-HIV-1,
pubmed-meshheading:1381907-Oligosaccharides,
pubmed-meshheading:1381907-Recombinant Proteins,
pubmed-meshheading:1381907-Vaccinia virus
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pubmed:year |
1992
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pubmed:articleTitle |
An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1 env gene recombinant vaccinia virus.
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pubmed:affiliation |
Department of Infectious Diseases, Hvidovre Hospital, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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