2026-06-14T06:44:13Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/77052025-06-09T14:59:16Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
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
funder
Instituto de Salud Carlos III
funder
Israel Science Foundation
2019-06-03T07:19:20Z
2019-06-03T07:19:20Z
2010-07
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
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.
eng
Multiple, non-conserved, internal viral ligands naturally presented by HLA-B27 in human respiratory syncytial virus-infected cells
research article
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URL
https://repisalud.isciii.es/bitstreams/4a74f9be-5cdc-4da7-8bec-bd1ec21b8c70/download
File
MD5
ecdc6c2f2003e02345ac28fb787a1984
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application/pdf
MultipleNonConservedInternal_2010.pdf
URL
https://repisalud.isciii.es/bitstreams/ada3a260-c5c2-4eaf-84c3-ec76c0c492ec/download
File
MD5
aa7fd4012133d60b84bf356b9b014dda
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text/plain
MultipleNonConservedInternal_2010.pdf.txt