| http://purl.uniprot.org/citations/19789338 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19789338 | http://www.w3.org/2000/01/rdf-schema#comment | "Immunogenicity of tumor-associated antigens (TAA) is often weak because many TAA are autoantigens for which the T-cell repertoire is sculpted by tolerance mechanisms. Substitutions at main anchor positions to increase the complementarity between the peptide and the MHC class I (MHC-I) binding cleft constitute a common procedure to improve binding capacity and immunogenicity of TAA. However, such alterations are tailored for each MHC-I allele and may recruit different CTL specificities through conformational changes in the targeted peptides. Comparative analysis of substituted melanoma-differentiation antigen gp100 in complex with H-2D(b) revealed that combined introduction of glycine and proline residues at the nonanchor positions 2 and 3, respectively, resulted in an agonistic altered peptide with dramatically enhanced binding affinity, stability, and immunogenicity of this TAA. Peptide vaccination using the p2Gp3P-altered peptide version of gp100 induced high frequencies of melanoma-specific CTL in the endogenous CD8+ repertoire. Crystal structure analysis of MHC/peptide complexes revealed that the conformation of the modified p2Gp3P-peptide was similar to the wild-type peptide, and indicated that this mimotope was stabilized through interactions between peptide residue p3P and the tyrosine residue Y159 that is conserved among most known MHC-I molecules throughout mammalian species. Our results may provide an alternative approach to enhance MHC stabilization capacity and immunogenicity of low-affinity peptides for induction of robust tumor-specific CTL."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.org/dc/terms/identifier | "doi:10.1158/0008-5472.can-09-1724"xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "Achour A."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "Badia-Martinez D."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "Offringa R."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "Sluijter M."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "van Hall T."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/author | "van Stipdonk M.J."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/name | "Cancer Res"xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/pages | "7784-7792"xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/title | "Design of agonistic altered peptides for the robust induction of CTL directed towards H-2Db in complex with the melanoma-associated epitope gp100."xsd:string |
| http://purl.uniprot.org/citations/19789338 | http://purl.uniprot.org/core/volume | "69"xsd:string |
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