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To investigate how early events in antigen processing affect the repertoire of peptides presented by MHC class I molecules, we compared the presentation of the influenza A nucleoprotein epitope 265-273 by HLA-A3 class I molecules in human and mouse cells. Mouse cells that express HLA-A3 failed to present the NP265-273 peptide when contained within the full-length nucleoprotein, to HLA-A3-restricted human cytotoxic T lymphocytes. However, when the epitope was generated directly in the cytosol using a recombinant vaccinia virus that expressed the nonamer peptide, mouse cells were recognized by HLA-A3-restricted CTL. Poor transport of the peptide by mouse TAP was not responsible for the defect as co-infection of mouse cells with recombinant vaccinia viruses encoding the full-length nucleoprotein and the human TAP1 and TAP2 peptide transporter complex failed to restore presentation. These results therefore demonstrate a differential processing of the influenza nucleoprotein in mouse and human cells. This polymorphism influences the repertoire of peptides presented by MHC class I molecules at the cell surface.

Original publication




Journal article


Eur J Immunol

Publication Date





625 - 635


ATP Binding Cassette Transporter, Subfamily B, Member 2, ATP Binding Cassette Transporter, Subfamily B, Member 3, ATP-Binding Cassette Transporters, Animals, Antigen Presentation, Antigens, Viral, Biological Transport, Endoplasmic Reticulum, Epitopes, HLA-A3 Antigen, Humans, Influenza A virus, L Cells (Cell Line), Mast-Cell Sarcoma, Mice, Nucleoproteins, RNA-Binding Proteins, T-Lymphocytes, Cytotoxic, Transfection, Tumor Cells, Cultured, Viral Core Proteins