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Tapasin facilitatio...
Tapasin facilitation of MHC-I separates closely related allomorphs, is strongly influenced by peptide length and depends on stability
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- Geironson Ulfsson, Linda (författare)
- Lund University,Lunds universitet,Avdelningen för molekylär hematologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Molecular Hematology (DMH),Department of Laboratory Medicine,Faculty of Medicine
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- Thuring, Camilla (författare)
- Lund University,Lunds universitet,Adaptivt immunförsvar,Forskargrupper vid Lunds universitet,Adaptive Immunity,Lund University Research Groups
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Harndahl, Mikkel (författare)
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Rasmussen, M. (författare)
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Buus, Søren (författare)
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Røder, Gustav (författare)
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- Paulsson, Kajsa (författare)
- Lund University,Lunds universitet,Antigen presentation,Forskargrupper vid Lunds universitet,Antigen Presentation,Lund University Research Groups
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(creator_code:org_t)
- 2013
- 2013
- Engelska 1 s.
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Ingår i: ; , s. 83-83
- Relaterad länk:
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http://www.ici2013.o...
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https://lup.lub.lu.s...
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Abstract
Ämnesord
Stäng
- Only a small fraction of the peptides inside a cell are eventually presented by HLA-I on the cell surface. The presented peptides have HLA-I allomorph-specific motifs and length restrictions. Tapasin influences HLA-I antigen presentation both qualitatively and quantitatively to different degrees depending on both peptide sequence and HLA-I allomorph. The tapasin-dependence in cellular context has been shown to correspond to the facilitation of peptide- HLA-I complex formation by the first 87 amino acids of tapasin (Tpn1- 87) (i.e., tapasin-facilitation = Bmax Tpn1-87/Bmax Ctrl) in a biochemical assay. Both peptide length and tapasin-facilitation are important for HLA-I antigen presentation and we here set out to study if these two parameters relate to each other. We used a luminescent oxygen channeling assay and seven different peptide libraries (X7- X13) to study 16 HLA-A and -B allomorphs and the results show a broad spectrum of tapasin-facilitation of HLA-I allomorphs and that HLA-A allomorphs were generally less restricted than -B allomorphs83to peptides of the classical lengths of 8-10 amino acids. Since both stability and tapasin-facilitation have been suggested as discriminators of immunogenic peptides we used a scintillation proximity based assay to study the stability of peptide-HLA-I complexes formed with peptides of different lengths. The results demonstrate an inverse correlation between tapasin-facilitation and stability valid for different peptide mixes of specific lengths but also on the level of HLA-I allomorphs, suggesting that molecules of poor stability are either not in a conformation that allows tapasin to interact or have a conformation where association has no effect.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Nyckelord
- tapasin
- peptide
- HLA-I
- MHC-I
- antigen presentation
Publikations- och innehållstyp
- kon (ämneskategori)
- ref (ämneskategori)