Source:http://linkedlifedata.com/resource/pubmed/id/11300471
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rdf:type | |
lifeskim:mentions |
umls-concept:C0085358,
umls-concept:C0162326,
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umls-concept:C2825965,
umls-concept:C2911692
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pubmed:issue |
3 Suppl
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pubmed:dateCreated |
2001-4-12
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pubmed:abstractText |
We have shown previously that HLA-A*0201 melanoma patients can frequently develop a CTL response to the cancer testis antigen NY-ESO-1. In the present study, we have analyzed in detail the relative antigenicity and in vitro immunogenicity of natural and modified NY-ESO-1 peptide sequences. The results of this analysis revealed that, although suboptimal for binding to the HLA-A*0201 molecule, peptide NY-ESO-1 157-165 is, among natural sequences, very efficiently recognized by specific CTL clones derived from three melanoma patients. In contrast, peptides NY-ESO-1 157-167 and NY-ESO-1 155-163, which bind very strongly to HLA-A*0201, are recognized less efficiently. In agreement with previous data, substitution of peptide NY-ESO-1 157-165 COOH-terminal C with various other amino acids resulted in a significantly increased binding to HLA-A*0201 molecules as well as in an increased CTL recognition, although variable at the clonal level. Among natural peptides, NY-ESO-1 157-165 and NY-ESO-1 157-167 exhibited good in vitro immunogenicity, whereas peptide NY-ESO-1 155-163 was poorly immunogenic. The fine specificity of interaction between peptide NY-ESO-1 C165A, HLA-A*0201, and T-cell receptor was analyzed at the molecular level using a series of variant peptides containing single alanine substitutions. The findings reported here have significant implications for the formulation of NY-ESO-1-based vaccines as well as for the monitoring of either natural or vaccine-induced NY-ESO-1-specific CTL responses in cancer patients.
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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/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CTAG1B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1078-0432
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
766s-772s
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11300471-Antigens,
pubmed-meshheading:11300471-Antigens, Neoplasm,
pubmed-meshheading:11300471-Binding, Competitive,
pubmed-meshheading:11300471-CD8-Positive T-Lymphocytes,
pubmed-meshheading:11300471-Cell Separation,
pubmed-meshheading:11300471-Dose-Response Relationship, Drug,
pubmed-meshheading:11300471-Flow Cytometry,
pubmed-meshheading:11300471-HLA-A2 Antigen,
pubmed-meshheading:11300471-Humans,
pubmed-meshheading:11300471-Interferon-gamma,
pubmed-meshheading:11300471-Melanoma,
pubmed-meshheading:11300471-Membrane Proteins,
pubmed-meshheading:11300471-Microscopy, Fluorescence,
pubmed-meshheading:11300471-Peptides,
pubmed-meshheading:11300471-Protein Binding,
pubmed-meshheading:11300471-Proteins,
pubmed-meshheading:11300471-Tumor Cells, Cultured
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pubmed:year |
2001
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pubmed:articleTitle |
CD8+ T-cell response to NY-ESO-1: relative antigenicity and in vitro immunogenicity of natural and analogue sequences.
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pubmed:affiliation |
Division of Clinical Onco-Immunology, Ludwig Institute for Cancer Research, Lausanne Branch, Centre Hospitalier Universitaire Vaudois, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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