2024-03-29T14:36:56Zhttp://repisalud.isciii.es/oai/requestoai:repisalud.isciii.es:20.500.12105/106592023-02-27T18:16:03Zcom_20.500.12105_2060com_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_2061
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.
0818-9641
http://hdl.handle.net/20.500.12105/10659
20975736
10.1038/icb.2010.125
1440-1711
Immunology and cell biology
Unusual viral ligand with alternative interactions is presented by HLA-Cw4 in human respiratory syncytial virus-infected cells.