Multiple, Non-conserved, Internal Viral Ligands Naturally Presented by HLA-B27 in Human Respiratory Syncytial Virus-infected Cells
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 s...
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| Veröffentlicht in: | Molecular & cellular proteomics 2010-07, Vol.9 (7), p.1533-1539 |
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| container_title | Molecular & cellular proteomics |
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| creator | Infantes, Susana Lorente, Elena Barnea, Eilon Beer, Ilan Cragnolini, Juan José García, Ruth Lasala, Fátima Jiménez, Mercedes Admon, Arie López, Daniel |
| description | 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. |
| doi_str_mv | 10.1074/mcp.M900508-MCP200 |
| format | Article |
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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. 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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. 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| subjects | Amino Acid Sequence Animals Antigen Presentation - immunology Antigens, Viral - chemistry Antigens, Viral - genetics Antigens, Viral - immunology Histocompatibility Antigens Class I - genetics Histocompatibility Antigens Class I - immunology Humans Ligands Molecular Sequence Data Peptides - chemistry Peptides - genetics Peptides - immunology Respiratory Syncytial Virus Infections - immunology Respiratory Syncytial Virus, Human - immunology Spectrometry, Mass, Electrospray Ionization - methods T-Lymphocytes, Cytotoxic - immunology |
| title | Multiple, Non-conserved, Internal Viral Ligands Naturally Presented by HLA-B27 in Human Respiratory Syncytial Virus-infected Cells |
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