Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/12559
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dc.contributor.authorZanker, Damienen
dc.contributor.authorQuinn, Kylieen
dc.contributor.authorWaithman, Jasonen
dc.contributor.authorLata, Roleenen
dc.contributor.authorMurphy, Rogeren
dc.contributor.authorLa Gruta, Nicole Louiseen
dc.contributor.authorChen, Weisanen
dc.date.accessioned2015-05-16T02:16:22Z
dc.date.available2015-05-16T02:16:22Z
dc.date.issued2015-01-06en
dc.identifier.citationImmunology and Cell Biology 2015; 93(5): 500-7en
dc.identifier.govdoc25559620en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/12559en
dc.description.abstractT-cell repertoire is selected according to self peptide-MHC (major histocompatibility complex) complexes in the thymus. Although most peripheral T cells recognize specific pathogen-derived peptides complexed to self-MHC exclusively, some possess cross-reactivity to other self or foreign peptides presented by self-MHC molecules; a phenomenon often termed T-cell receptor (TCR) promiscuity or degeneracy. TCR promiscuity has been attributed to various autoimmune conditions. On the other hand, it is considered a mechanism for a relatively limited TCR repertoire to deal with a potentially much larger antigenic peptide repertoire. Such property has also been utilized to bypass self-tolerance for cancer vaccine development. Although many studies explored such degeneracy for peptide of the same length, few studies reported such properties for peptides of different length. In this study, we finely characterized the CD8(+) T-cell response specific for a 11mer peptide derived from influenza A viral polymerase basic protein 2. The short-term T-cell line, despite possessing highly biased TCR, was able to react with multiple peptides of different length sharing the same core sequence. Out data clearly showed the importance of detailed and quantitative assessments for such T-cell specificity. Our data also emphasize the importance of biochemical demonstration of the naturally presented minimal peptide.Immunology and Cell Biology advance online publication, 6 January 2015; doi:10.1038/icb.2014.113.en
dc.language.isoenen
dc.titleT cells recognizing a 11mer influenza peptide complexed to H-2D(b) show promiscuity for peptide length.en
dc.typeJournal Articleen
dc.identifier.journaltitleImmunology and cell biologyen
dc.identifier.affiliationDepartment of Microbiology and Immunology, Melbourne University, Parkville, Victoria, Australiaen
dc.identifier.affiliationTelethon Institute for Child Health Research, Subiaco, Western Australia, Australiaen
dc.identifier.affiliationT Cell Laboratory, School of Molecular Science, La Trobe University, Bundoora, Victoria, Australiaen
dc.identifier.affiliationDepartment of Medicine, Monash Medical Centre, Clayton, Victoria, Australiaen
dc.identifier.affiliationLudwig Institute for Cancer Research, Austin Health, Heidelberg, Victoria, Australiaen
dc.identifier.doi10.1038/icb.2014.113en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/25559620en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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