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Proline substitution independently enhances H-2D(b) complex stabilization and TCR recognition of melanoma-associated peptides
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2013 (English)In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 43, no 11, 3051-3060 p.Article in journal (Refereed) Published
Abstract [en]

The immunogenicity of H-2D(b) (D-b) restricted epitopes can be significantly increased by substituting peptide position 3 to a proline (p3P). The p3P modification enhances MHC stability without altering the conformation of the modified epitope allowing for T-cell cross-reactivity with the native peptide. The present study reveals how specific interactions between p3P and the highly conserved MHC heavy chain residue Y159 increase the stability of D-b in complex with an optimized version of the melanoma-associated epitope gp100(25-33). Furthermore, the p3P modification directly increased the affinity of the D-b/gp100(25-33)-specific T-cell receptor (TCR) pMel. Surprisingly, the enhanced TCR binding was independent from the observed increased stability of the optimized D-b/gp100(25-33) complex and from the interactions formed between p3P and Y159, indicating a direct effect of the p3P modification on TCR recognition.

Place, publisher, year, edition, pages
2013. Vol. 43, no 11, 3051-3060 p.
Keyword [en]
MHC, Structural Biology, T-cell epitope, TCR, Tumor antigen
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URN: urn:nbn:se:kth:diva-140169DOI: 10.1002/eji.201343456ISI: 000328074000012ScopusID: 2-s2.0-84884337225OAI: diva2:689252
Swedish Research CouncilSwedish Cancer Society

QC 20140120

Available from: 2014-01-20 Created: 2014-01-17 Last updated: 2014-01-20Bibliographically approved

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Nygren, Per-Åke
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Protein Technology
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