Please use this identifier to cite or link to this item: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.
Infantes, Susana ISCIII | Lorente, Elena ISCIII | Cragnolini, Juan José | Ramos, Manuel ISCIII | Garcia, Ruth ISCIII | Jimenez, Mercedes ISCIII | Iborra, Salvador ISCIII | Val, Margarita del ISCIII | Lopez, Daniel ISCIII
Immunol Cell Biol . 2011 May;89(4):558-65.
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.
Ligands | Animals | Antigens, Viral | Cell Line | HLA-C Antigens | Histocompatibility Antigens Class I | Humans | Mice | Molecular Dynamics Simulation | Oligopeptides | Peptides | Protein Binding | Protein Conformation | Respiratory Syncytial Virus Infections | Respiratory Syncytial Virus, Human
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