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00925njm 22002777a 4500 dc Infantes, Susana author Lorente, Elena author Barnea, Eilon author Beer, Ilan author Cragnolini, Juan José author Garcia, Ruth author Lasala, Fátima author Jimenez, Mercedes author Admon, Arie author Lopez, Daniel author 2010-07 Cytotoxic T lymphocyte (CTL)-mediated death of virus-infected cells requires prior recognition of short viral peptide antigens that are presented by human leukocyte antigen (HLA) class I molecules on the surface of infected cells. The CTL response is critical for the clearance of human respiratory syncytial virus (HRSV) infection. Using mass spectrometry analysis of complex HLA-bound peptide pools isolated from large amounts of HRSV-infected cells, we identified nine naturally processed HLA-B27 ligands. The isolated peptides are derived from six internal, not envelope, proteins of the infective virus. The sequences of most of these ligands are not conserved between different HRSV strains, suggesting a mechanism to explain recurrent infection with virus of different HRSV antigenic subgroups. In addition, these nine ligands represent a significant fraction of the proteome of this virus, which is monitored by the same HLA class I allele. These data have implications for vaccine development as well as for analysis of the CTL response. Mol Cell Proteomics. 2010;9(7):1533-9. 10.1074/mcp.M900508-MCP200 1535-9484 1535-9476 Molecular & cellular proteomics : MCP 20081153 http://hdl.handle.net/20.500.12105/7705 Multiple, non-conserved, internal viral ligands naturally presented by HLA-B27 in human respiratory syncytial virus-infected cells