Tapasin facilitation of natural HLA-A and -B allomorphs is strongly influenced by peptide length, depends on stability, and separates closely related allomorphs.
Identifieur interne : 001E97 ( Main/Exploration ); précédent : 001E96; suivant : 001E98Tapasin facilitation of natural HLA-A and -B allomorphs is strongly influenced by peptide length, depends on stability, and separates closely related allomorphs.
Auteurs : Linda Geironson [Suède] ; Camilla Thuring ; Mikkel Harndahl ; Michael Rasmussen ; S Ren Buus ; Gustav R Der ; Kajsa M. PaulssonSource :
- Journal of immunology (Baltimore, Md. : 1950) [ 1550-6606 ] ; 2013.
Descripteurs français
- KwdFr :
- Antigènes HLA-A (), Antigènes HLA-A (immunologie), Antigènes HLA-A (métabolisme), Antigènes HLA-B (), Antigènes HLA-B (immunologie), Antigènes HLA-B (métabolisme), Humains, Liaison aux protéines, Peptides (), Peptides (immunologie), Peptides (métabolisme), Pliage des protéines, Protéines de transport membranaire (métabolisme), Présentation d'antigène (immunologie), Stabilité protéique.
- MESH :
English descriptors
- KwdEn :
- Antigen Presentation (immunology), HLA-A Antigens (chemistry), HLA-A Antigens (immunology), HLA-A Antigens (metabolism), HLA-B Antigens (chemistry), HLA-B Antigens (immunology), HLA-B Antigens (metabolism), Humans, Membrane Transport Proteins (metabolism), Peptides (chemistry), Peptides (immunology), Peptides (metabolism), Protein Binding, Protein Folding, Protein Stability.
- MESH :
- chemical , chemistry : HLA-A Antigens, HLA-B Antigens, Peptides.
- immunology : Antigen Presentation, HLA-A Antigens, HLA-B Antigens, Peptides.
- chemical , metabolism : HLA-A Antigens, HLA-B Antigens, Membrane Transport Proteins, Peptides.
- Humans, Protein Binding, Protein Folding, Protein Stability.
Abstract
Despite an abundance of peptides inside a cell, only a small fraction is ultimately presented by HLA-I on the cell surface. The presented peptides have HLA-I allomorph-specific motifs and are restricted in length. So far, detailed length studies have been limited to few allomorphs. Peptide-HLA-I (pHLA-I) complexes of different allomorphs are qualitatively and quantitatively influenced by tapasin to different degrees, but again, its effect has only been investigated for a small number of HLA-I allomorphs. Although both peptide length and tapasin dependence are known to be important for HLA-I peptide presentation, the relationship between them has never been studied. In this study, we used random peptide libraries from 7- to 13-mers and studied binding in the presence and absence of a recombinant truncated form of tapasin. The data show that HLA-I allomorphs are differentially affected by tapasin, different lengths of peptides generated different amounts of pHLA-I complexes, and HLA-A allomorphs are generally less restricted than HLA-B allomorphs to peptides of the classical length of 8-10 aa. We also demonstrate that tapasin facilitation varies for different peptide lengths, and that the correlation between high degree of tapasin facilitation and low stability is valid for different random peptide mixes of specific lengths. In conclusion, these data show that tapasin has specificity for the combination of peptide length and HLA-I allomorph, and suggest that tapasin promotes formation of pHLA-I complexes with high on and off rates, an important intermediary step in the HLA-I maturation process.
DOI: 10.4049/jimmunol.1201741
PubMed: 23980206
Affiliations:
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Paulsson</name></author></analytic><series><title level="j">Journal of immunology (Baltimore, Md. : 1950)</title><idno type="eISSN">1550-6606</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antigen Presentation (immunology)</term><term>HLA-A Antigens (chemistry)</term><term>HLA-A Antigens (immunology)</term><term>HLA-A Antigens (metabolism)</term><term>HLA-B Antigens (chemistry)</term><term>HLA-B Antigens (immunology)</term><term>HLA-B Antigens (metabolism)</term><term>Humans</term><term>Membrane Transport Proteins (metabolism)</term><term>Peptides (chemistry)</term><term>Peptides (immunology)</term><term>Peptides (metabolism)</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Stability</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antigènes HLA-A ()</term><term>Antigènes HLA-A (immunologie)</term><term>Antigènes HLA-A (métabolisme)</term><term>Antigènes HLA-B ()</term><term>Antigènes HLA-B (immunologie)</term><term>Antigènes HLA-B (métabolisme)</term><term>Humains</term><term>Liaison aux protéines</term><term>Peptides ()</term><term>Peptides (immunologie)</term><term>Peptides (métabolisme)</term><term>Pliage des protéines</term><term>Protéines de transport membranaire (métabolisme)</term><term>Présentation d'antigène (immunologie)</term><term>Stabilité protéique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>HLA-A Antigens</term><term>HLA-B Antigens</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes HLA-A</term><term>Antigènes HLA-B</term><term>Peptides</term><term>Présentation d'antigène</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Antigen Presentation</term><term>HLA-A Antigens</term><term>HLA-B Antigens</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>HLA-A Antigens</term><term>HLA-B Antigens</term><term>Membrane Transport Proteins</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigènes HLA-A</term><term>Antigènes HLA-B</term><term>Peptides</term><term>Protéines de transport membranaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Stability</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Antigènes HLA-A</term><term>Antigènes HLA-B</term><term>Humains</term><term>Liaison aux protéines</term><term>Peptides</term><term>Pliage des protéines</term><term>Stabilité protéique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Despite an abundance of peptides inside a cell, only a small fraction is ultimately presented by HLA-I on the cell surface. The presented peptides have HLA-I allomorph-specific motifs and are restricted in length. So far, detailed length studies have been limited to few allomorphs. Peptide-HLA-I (pHLA-I) complexes of different allomorphs are qualitatively and quantitatively influenced by tapasin to different degrees, but again, its effect has only been investigated for a small number of HLA-I allomorphs. Although both peptide length and tapasin dependence are known to be important for HLA-I peptide presentation, the relationship between them has never been studied. In this study, we used random peptide libraries from 7- to 13-mers and studied binding in the presence and absence of a recombinant truncated form of tapasin. The data show that HLA-I allomorphs are differentially affected by tapasin, different lengths of peptides generated different amounts of pHLA-I complexes, and HLA-A allomorphs are generally less restricted than HLA-B allomorphs to peptides of the classical length of 8-10 aa. We also demonstrate that tapasin facilitation varies for different peptide lengths, and that the correlation between high degree of tapasin facilitation and low stability is valid for different random peptide mixes of specific lengths. In conclusion, these data show that tapasin has specificity for the combination of peptide length and HLA-I allomorph, and suggest that tapasin promotes formation of pHLA-I complexes with high on and off rates, an important intermediary step in the HLA-I maturation process. </div></front></TEI><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Buus, S Ren" sort="Buus, S Ren" uniqKey="Buus S" first="S Ren" last="Buus">S Ren Buus</name><name sortKey="Harndahl, Mikkel" sort="Harndahl, Mikkel" uniqKey="Harndahl M" first="Mikkel" last="Harndahl">Mikkel Harndahl</name><name sortKey="Paulsson, Kajsa M" sort="Paulsson, Kajsa M" uniqKey="Paulsson K" first="Kajsa M" last="Paulsson">Kajsa M. Paulsson</name><name sortKey="R Der, Gustav" sort="R Der, Gustav" uniqKey="R Der G" first="Gustav" last="R Der">Gustav R Der</name><name sortKey="Rasmussen, Michael" sort="Rasmussen, Michael" uniqKey="Rasmussen M" first="Michael" last="Rasmussen">Michael Rasmussen</name><name sortKey="Thuring, Camilla" sort="Thuring, Camilla" uniqKey="Thuring C" first="Camilla" last="Thuring">Camilla Thuring</name></noCountry><country name="Suède"><noRegion><name sortKey="Geironson, Linda" sort="Geironson, Linda" uniqKey="Geironson L" first="Linda" last="Geironson">Linda Geironson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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