Proceedings of the National Academy of Sciences · 2004 · 181 citations · 36 references
Life SciencesCell BiologyImmunologyAdaptive ImmunityCellular ImmunologyVaccine ImmunologyAntigen PresentationAntigen ProcessingAntigen RecognitionCell-mediated ImmunityHuman Leukocyte Antigen SystemMajor Histocompatibility ComplexClass I Histocompatibility AntigensMajor Histocompatibility Complex (Mhc) PresentationMajor Histocompatibility Complex Class I PresentationMhc Class I MoleculesPeptide Antigen PresentationPeptide EpitopesTapasin FunctionVaccination Strategies
Understanding how peptides are selected for presentation by MHC class I is crucial to vaccination strategies based on cytotoxic T lymphocyte priming. We have studied this selection of the MHC class I peptide repertoire in terms of the presentation of a series of individual peptides with a wide range of binding to MHC class I. This series was expressed as minigenes, and the presentation of each peptide variant was determined with the same MHC class I peptide-specific antibody. In wild-type cells, the hierarchy of presentation followed peptide half-life. This hierarchy broke down in cells lacking tapasin but not in cells lacking calreticulin or in cells lacking transporter associated with antigen processing-associated ERp57. We demonstrate a key role for tapasin in shaping the MHC class I peptide repertoire, as enhancement of presentation in the presence of tapasin correlated with peptide half-life.
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Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
Kirsten Falk, Olaf Rötzschke, Stefan Stevanovié et al. · Nature · 1991 · 2.4K citations
Empty MHC class I molecules come out in the cold
Hans-Gustaf Ljunggren, Nico J. Stam, Claes Öhlén et al. · Nature · 1990 · 936 citations