Source:http://linkedlifedata.com/resource/pubmed/id/10733926
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-5-4
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pubmed:abstractText |
The synthetic peptide comprising the 317-341 region of human influenza A virus (H1N1 subtype) hemagglutinin elicits peptide-specific antibody and helper T cell responses and confers protection against lethal virus infection. Molecular mapping of the 317-329 region, which encompasses the epitope recognized by peptide-specific T cells, revealed that the minimal size required for T cell activation was the 317-326 segment. The most likely peptide alignment, which placed 320Leu to pocket 1 of the I-E(d) peptide binding groove, was predicted by molecular mechanics calculations performed with the parental and with the Ala-substituted analogs. In line with the prediction data, the results of the peptide binding assay, where the relative binding efficiency to I-E(d) molecules expressed on the surface of antigen-presenting cells was monitored, identified the 320-326 core sequence interacting with the major histocompatibility class II peptide binding groove. Functional analysis of Ala-substituted variants by functional assays and by calculating the surface-accessible areas of the single peptidic amino acids in the I-E(d)-peptide complexes demonstrated that 324Pro is a primary contact residue for the T cell receptor. Our results show that this type of analysis offers a suitable tool for molecular mapping of helper T cell epitopes and thus provides valuable data for subunit vaccine design.
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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/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinin Glycoproteins...,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/I-E-antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
190-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10733926-Alanine,
pubmed-meshheading:10733926-Computer Simulation,
pubmed-meshheading:10733926-Epitope Mapping,
pubmed-meshheading:10733926-Epitopes,
pubmed-meshheading:10733926-Hemagglutinin Glycoproteins, Influenza Virus,
pubmed-meshheading:10733926-Histocompatibility Antigens Class II,
pubmed-meshheading:10733926-Influenza A virus,
pubmed-meshheading:10733926-Interleukin-2,
pubmed-meshheading:10733926-Lymphocyte Activation,
pubmed-meshheading:10733926-Mutagenesis, Site-Directed,
pubmed-meshheading:10733926-Peptide Fragments,
pubmed-meshheading:10733926-Protein Binding,
pubmed-meshheading:10733926-Receptors, Antigen, T-Cell,
pubmed-meshheading:10733926-T-Lymphocytes, Helper-Inducer
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pubmed:year |
2000
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pubmed:articleTitle |
Mapping of a protective helper T cell epitope of human influenza A virus hemagglutinin.
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pubmed:affiliation |
Department of Immunology, L. Eötvös University, Göd, Hungary.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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