Johnstone, CarolinaLorente, ElenaBarriga, AlejandroBarnea, EilonInfantes, SusanaLemonnier, François ADavid, Chella SAdmon, ArieLopez, Daniel2019-11-142019-11-142015-04Mol Cell Proteomics. 2015 Apr;14(4):893-904. doi: 10.1074/mcp.M114.045401. Epub 2015 Jan 29.1535-9476http://hdl.handle.net/20.500.12105/8585The cytotoxic T-lymphocyte-mediated killing of virus-infected cells requires previous recognition of short viral antigenic peptides bound to human leukocyte antigen class I molecules that are exposed on the surface of infected cells. The cytotoxic T-lymphocyte response is critical for the clearance of human respiratory syncytial virus infection. In this study, naturally processed viral human leukocyte antigen class I ligands were identified with mass spectrometry analysis of complex human leukocyte antigen-bound peptide pools isolated from large amounts of human respiratory syncytial virus-infected cells. Acute antiviral T-cell response characterization showed that viral transcription determines both the immunoprevalence and immunodominance of the human leukocyte antigen class I response to human respiratory syncytial virus. These findings have clear implications for antiviral vaccine design.engAMhttp://creativecommons.org/licenses/by-nc-sa/4.0/Amino Acid SequenceAnimalsAntigen PresentationCell ExtractsCell LineHistocompatibility Antigens Class IHumansImmunity, CellularImmunodominant EpitopesLigandsMice, TransgenicMolecular Sequence DataPeptidesProteomeRespiratory Syncytial Virus, HumanT-LymphocytesTandem Mass SpectrometryTranscription, GeneticAtribución-NoComercial-CompartirIgual 4.0 Internacional25635267144893-90410.1074/mcp.M114.0454011535-9484Molecular & cellular proteomics : MCPopen access