Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/1663
DC FieldValueLanguage
dc.contributor.authorScala, Viviana-
dc.contributor.authorCasani, Daniela-
dc.contributor.authorCostantini, Susan-
dc.contributor.authorFacchiano, Angelo M.-
dc.contributor.authorMazzini, Massimo-
dc.contributor.authorScapigliati, Giuseppe-
dc.contributor.authorBuonocore, Francesco-
dc.date.accessioned2011-03-24T15:01:50Z-
dc.date.available2011-03-24T15:01:50Z-
dc.date.issued2008it
dc.identifier.citationRandelli, E. et al. 2008. T cell receptor beta chain from sea bream (Sparus aurata): Molecular cloning, expression and modelling of the complexes with MHC class I. "Molecular Immunology" 45(7): 2017-2027it
dc.identifier.issn0161-5890-
dc.identifier.urihttp://hdl.handle.net/2067/1663-
dc.descriptionL'articolo è disponibile sul sito dell'editore http://www.sciencedirect.com/it
dc.description.abstractThe T cell receptor is a fundamental mediator of the adaptive immune responses, since TR on T cells recognize foreign structures (peptides derived from processed antigens) bound to the major histocompatibility complex (MHC) on APC cells. In the present study, we report the cloning of six TRB chains cDNA sequences from gilthead sea bream (Sparus aurata), a fish of high economical impact in South Mediterranean aquaculture. The V-BETA domains have the canonical features of known teleost and mammalian TR V-BETA domains and have been divided in four different subgroups. A multiple alignment of the six sea bream TRB chains with other known TRB sequences was assembled and showed the conservation of the four cysteine residues involved in disulphide bonds and of some amino acids with an important role in the assembly and signalling of the TR /CD3 complex. Real-time PCR analysis was used to investigate TRB basal expression, that was maximum in the thymus followed by gut, and TRB in vitro expression after stimulation with LPS or PHA-L at 4 and 24 h (only the 4 h stimulation with LPS gave an significant effect). Moreover, the 3D structures of sea bream TRB chains and MHC-I were predicted by homology modelling with the final aim to investigate the interaction surface in the V-BETA/MHC-I complexes.it
dc.language.isoenit
dc.publisherElsevierit
dc.subjectFish Immunologyit
dc.subjectMolecular Biologyit
dc.subjectT-cell antigen receptorit
dc.subjectTcRβit
dc.subjectSparus auratait
dc.subjectReal time PCRit
dc.subject3D structureit
dc.subjectClass I MHCit
dc.subjectTcRβ/MHC complexesit
dc.titleT cell receptor beta chain from sea bream (Sparus aurata): molecular cloning, expression and modelling of the complexes with MHC class Iit
dc.typeArticleit
dc.identifier.doi10.1016/j.molimm.2007.10.027it
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.cerifentitytypePublications-
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