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rdf:type |
|
|
lifeskim:mentions |
|
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pubmed:issue |
9
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pubmed:dateCreated |
1991-11-19
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pubmed:abstractText |
The HIV envelope protein gp120 is heavily glycosylated, having 55% of its molecular mass contributed by N-linked carbohydrates. We investigated the role of N-glycosylation in presentation of HIV-gp120 to T cells. T cell clones obtained from humans immunized with a recombinant nonglycosylated form of HIV-gp120 (env 2-3) were studied for their ability to recognize both env 2-3 and glycosylated gp120. We found that 20% of CD4+ T cell clones specific for env 2-3 fail to respond to glycosylated gp120 of the same HIV isolate. Using synthetic peptides, we mapped one of the epitopes recognized by such clones to the sequence 292-300 (NESVAINCT), which contains two asparagines that are glycosylated in the native gp120. These findings suggest that N-linked carbohydrates within an epitope can function as hindering structures that limit Ag recognition by T lymphocytes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1767
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:day |
1
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|
pubmed:volume |
147
|
|
pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
3128-32
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1717587-Amino Acid Sequence,
pubmed-meshheading:1717587-CD4-Positive T-Lymphocytes,
pubmed-meshheading:1717587-Epitopes,
pubmed-meshheading:1717587-Glycoproteins,
pubmed-meshheading:1717587-Glycosylation,
pubmed-meshheading:1717587-HIV Antigens,
pubmed-meshheading:1717587-HIV Envelope Protein gp120,
pubmed-meshheading:1717587-HIV-1,
pubmed-meshheading:1717587-Humans,
pubmed-meshheading:1717587-Molecular Sequence Data,
pubmed-meshheading:1717587-Protein Processing, Post-Translational,
pubmed-meshheading:1717587-Recombinant Proteins,
pubmed-meshheading:1717587-Structure-Activity Relationship
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|
pubmed:year |
1991
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|
pubmed:articleTitle |
N-glycosylation of HIV-gp120 may constrain recognition by T lymphocytes.
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pubmed:affiliation |
Department of Allergy/Immunology, Ciba-Geigy Ltd, Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
In Vitro
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