Identification of wild-type and mutant p53 peptides binding to HLA-A2 assessed by a peptide loading-deficient cell line assay and a novel major histocompatibility complex class I peptide binding assay.

@article{Stuber1994IdentificationOW,
  title={Identification of wild-type and mutant p53 peptides binding to HLA-A2 assessed by a peptide loading-deficient cell line assay and a novel major histocompatibility complex class I peptide binding assay.},
  author={Gyorgy Stuber and Gilah. Leder and W T Storkus and Michael T Lotze and S Cardenas Modrow and L{\'a}szl{\'o} A. Sz{\'e}kely and Hans Wolf and Eric Voice Klein and Klas K{\"a}rre and George Klein},
  journal={European journal of immunology},
  year={1994},
  volume={24 3},
  pages={
          765-8
        }
}
Mutations of the p53 gene are the most frequently observed genetic changes in human cancers; often leading to an overexpression of the wild-type (wt) p53 protein. Demonstrable T cell reactivity against tumor cells overexpressing wt or mutant p53-derived peptides could support the application of such epitopes in cancer immunotherapies. As the binding of peptide to MHC class I molecules is a prerequisite for antigen-specific T cell recognition, we evaluated the ability of wt and mutant p53… CONTINUE READING
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