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Sökning: WFRF:(van Hall Thorbald)

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1.
  • Kessler, Jan H., et al. (författare)
  • Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes
  • 2010
  • Ingår i: Nature Immunology. - : Springer Science and Business Media LLC. - 1529-2908 .- 1529-2916. ; 12:1, s. 45-53
  • Tidskriftsartikel (refereegranskat)abstract
    • Cytotoxic T lymphocytes (CTLs) recognize peptides presented by HLA class I molecules on the cell surface. The C terminus of these CTL epitopes is considered to be produced by the proteasome. Here we demonstrate that the cytosolic endopeptidases nardilysin and thimet oligopeptidase (TOP) complemented proteasome activity. Nardilysin and TOP were required, either together or alone, for the generation of a tumor-specific CTL epitope from PRAME, an immunodominant CTL epitope from Epstein-Barr virus protein EBNA3C, and a clinically important epitope from the melanoma protein MART-1. TOP functioned as C-terminal trimming peptidase in antigen processing, and nardilysin contributed to both the C-terminal and N-terminal generation of CTL epitopes. By broadening the antigenic peptide repertoire, nardilysin and TOP strengthen the immune defense against intracellular pathogens and cancer.
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2.
  • Uchtenhagen, Hannes, et al. (författare)
  • Proline substitution independently enhances H-2D(b) complex stabilization and TCR recognition of melanoma-associated peptides
  • 2013
  • Ingår i: European Journal of Immunology. - : Wiley. - 0014-2980 .- 1521-4141. ; 43:11, s. 3051-3060
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
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