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oai:repisalud.isciii.es:20.500.12105/106592024-09-27T20:00:52Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Infantes, Susana author Lorente, Elena author Cragnolini, Juan José author Ramos, Manuel author Garcia, Ruth author Jimenez, Mercedes author Iborra, Salvador author Val, Margarita del author Lopez, Daniel author 2011-05 Short 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. Immunol Cell Biol . 2011 May;89(4):558-65. 10.1038/icb.2010.125 1440-1711 0818-9641 Immunology and cell biology 20975736 http://hdl.handle.net/20.500.12105/10659 Unusual viral ligand with alternative interactions is presented by HLA-Cw4 in human respiratory syncytial virus-infected cells.