Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1996-2-23
|
| pubmed:abstractText |
Deglycosylation of viral glycoproteins has been suggested to influence the number of available T cell determinants and to increase T cell recognition of antigens. In this study, we have investigated whether T cell responses to the HIV-1 envelope glycoprotein gp160 were influenced by deletion of three N-glycans of the protein. Wild type (wt) and a mutated form of gp160 (gp160A123) lacking the three N-glycans in the C-terminal CD4-binding region efficiently induced antigen-specific T cell responses in mice of the H-2b, H-2d, and H-2k haplotypes. Further, T cells primed by either wt gp160 or gp160A123 were stimulated in vitro to a similar extent by the homologous and heterologous protein, indicating that deletion of the glycans did not affect the overall immunogenicity and antigenicity of gp160A123. Wild-type gp160 and gp160A123 induced comparable T cell responses to those of epitopes which with respect to the secondary structure of gp160 were distant from the deleted glycans. However, in mice of the H-2b haplotype, wt gp160 primed T cells which responded in vitro to a peptide containing one of the deleted N-glycosylation sites (Asn448), whereas T cells induced by gp160A123 were unable to recognize this peptide. Thus, deletion of the glycans abrogated the in vivo priming of T cells recognizing an epitope in close proximity to the deletion sites. Furthermore, enzymatically deglycosylated gp160 failed to induce a T cell response to this epitope. These results indicate that the in vivo generation of certain T cell determinants from glycoproteins is dependent on the glycosylation of the protein.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, env,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp160,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0042-6822
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
215
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
124-33
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8560759-Amino Acid Sequence,
pubmed-meshheading:8560759-Animals,
pubmed-meshheading:8560759-Antigens, CD4,
pubmed-meshheading:8560759-Asparagine,
pubmed-meshheading:8560759-CD4-Positive T-Lymphocytes,
pubmed-meshheading:8560759-Epitopes,
pubmed-meshheading:8560759-Female,
pubmed-meshheading:8560759-Gene Products, env,
pubmed-meshheading:8560759-Glycosylation,
pubmed-meshheading:8560759-HIV Envelope Protein gp160,
pubmed-meshheading:8560759-HIV-1,
pubmed-meshheading:8560759-Humans,
pubmed-meshheading:8560759-Mice,
pubmed-meshheading:8560759-Mice, Inbred BALB C,
pubmed-meshheading:8560759-Mice, Inbred C57BL,
pubmed-meshheading:8560759-Mice, Inbred CBA,
pubmed-meshheading:8560759-Molecular Sequence Data,
pubmed-meshheading:8560759-Polysaccharides,
pubmed-meshheading:8560759-Protein Precursors,
pubmed-meshheading:8560759-Species Specificity,
pubmed-meshheading:8560759-Structure-Activity Relationship
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
N-linked glycans in the CD4-binding domain of human immunodeficiency virus type 1 envelope glycoprotein gp160 are essential for the in vivo priming of T cells recognizing an epitope located in their vicinity.
|
| pubmed:affiliation |
Department of Veterinary Microbiology, College of Veterinary Medicine, Swedish University of Agricultural Sciences, Uppsala, Sweden.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|