Linked Life Data

19157553

Source:http://linkedlifedata.com/resource/pubmed/id/19157553

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8-9
pubmed:dateCreated
2009-4-20
pubmed:abstractText
The major ligands presented by MHC class I molecules after natural antigen processing are peptides of eight to ten residues in length, and it is widely accepted that the binding preferences of MHC class I molecules play a dominant role in dictating this classic feature of antigen presentation. In this report, we have reassessed the peptide size specificity of class I human leukocyte antigens (HLAs). By lengthening previously defined T cell epitopes by central amino acid insertion, we demonstrate that the peptide length specificity of some common HLA class I alleles (HLA-B*3501, B*0702 and A*2402) is very broad, and includes peptides of up to 25 residues. These data suggest that the length limitation of naturally processed MHC class I-associated peptides is primarily controlled by peptide availability after antigen processing rather than the binding specificity of MHC class I molecules. Furthermore, the findings provide an explanation for recent reports highlighting that epitopes of >10 amino acids play a minor but significant role in virus-specific immune surveillance by CD8(+) T cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1872-9142
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1911-7
pubmed:dateRevised
2009-6-16
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The peptide length specificity of some HLA class I alleles is very broad and includes peptides of up to 25 amino acids in length.
pubmed:affiliation
Queensland Institute of Medical Research and Australian Centre for Vaccine Development, Herston, Brisbane, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't