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  <title>Unitus DSpace</title>
  <link rel="alternate" href="http://http://dspace.unitus.it:80" />
  <subtitle>The DSpace digital repository system captures, stores, indexes, preserves, and distributes digital research material.</subtitle>
  <id>http://http://dspace.unitus.it:80</id>
  <updated>2013-05-23T18:10:47Z</updated>
  <dc:date>2013-05-23T18:10:47Z</dc:date>
  <entry>
    <title>T cell receptor beta chain from sea bream (Sparus aurata): molecular cloning, expression and modelling of the complexes with MHC class I</title>
    <link rel="alternate" href="http://hdl.handle.net/2067/1663" />
    <author>
      <name>Scala, Viviana</name>
    </author>
    <author>
      <name>Casani, Daniela</name>
    </author>
    <author>
      <name>Costantini, Susan</name>
    </author>
    <author>
      <name>Facchiano, Angelo M.</name>
    </author>
    <author>
      <name>Mazzini, Massimo</name>
    </author>
    <author>
      <name>Scapigliati, Giuseppe</name>
    </author>
    <author>
      <name>Buonocore, Francesco</name>
    </author>
    <id>http://hdl.handle.net/2067/1663</id>
    <updated>2011-06-27T10:53:59Z</updated>
    <published>2007-12-31T23:00:00Z</published>
    <summary type="text">Title: T cell receptor beta chain from sea bream (Sparus aurata): molecular cloning, expression and modelling of the complexes with MHC class I
Authors: Scala, Viviana; Casani, Daniela; Costantini, Susan; Facchiano, Angelo M.; Mazzini, Massimo; Scapigliati, Giuseppe; Buonocore, Francesco
Abstract: The T cell receptor is a fundamental mediator of the adaptive immune responses, since TR    on T cells recognize foreign structures (peptides&#xD;
derived from processed antigens) bound to the major histocompatibility complex (MHC) on APC cells. In the present study, we report the cloning&#xD;
of six TRB chains cDNA sequences from gilthead sea bream (Sparus aurata), a fish of high economical impact in South Mediterranean aquaculture.&#xD;
The V-BETA domains have the canonical features of known teleost and mammalian TR V-BETA domains and have been divided in four different&#xD;
subgroups. A multiple alignment of the six sea bream TRB chains with other known TRB sequences was assembled and showed the conservation&#xD;
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&#xD;
TR   /CD3 complex. Real-time PCR analysis was used to investigate TRB basal expression, that was maximum in the thymus followed by gut,&#xD;
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).&#xD;
Moreover, the 3D structures of sea bream TRB chains and MHC-I were predicted by homology modelling with the final aim to investigate the&#xD;
interaction surface in the V-BETA/MHC-I complexes.
Description: L'articolo è disponibile sul sito dell'editore http://www.sciencedirect.com/</summary>
    <dc:date>2007-12-31T23:00:00Z</dc:date>
  </entry>
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