Infantes, SusanaLorente, ElenaCragnolini, Juan JoséRamos, ManuelGarcia, RuthJimenez, MercedesIborra, SalvadorVal, Margarita delLopez, Daniel2020-07-062020-07-062011-05Immunol Cell Biol . 2011 May;89(4):558-65.0818-9641http://hdl.handle.net/20.500.12105/10659Short viral antigens bound to human major histocompatibility complex (HLA) class I molecules are presented on infected cells. Vaccine development frequently relies on synthetic peptides to identify optimal HLA class I ligands. However, when natural peptides are analyzed, more complex mixtures are found. By immunoproteomics analysis, we identify in this study a physiologically processed HLA ligand derived from the human respiratory syncytial virus matrix protein that is very different from what was expected from studies with synthetic peptides. This natural HLA-Cw4 class I ligand uses alternative interactions to the anchor motifs previously described for its presenting HLA-Cw4 class I molecule. Finally, this octameric peptide shares its C-terminal core with the H-2D(b) nonamer ligand previously identified in the mouse model. These data have implications for the identification of antiviral cytotoxic T lymphocyte responses and for vaccine development.engAMhttp://creativecommons.org/licenses/by-nc-sa/4.0/LigandsAnimalsAntigens, ViralCell LineHLA-C AntigensHistocompatibility Antigens Class IHumansMiceMolecular Dynamics SimulationOligopeptidesPeptidesProtein BindingProtein ConformationRespiratory Syncytial Virus InfectionsRespiratory Syncytial Virus, HumanAtribución-NoComercial-CompartirIgual 4.0 Internacional20975736894558-6510.1038/icb.2010.1251440-1711Immunology and cell biologyopen access