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oai:repisalud.isciii.es:20.500.12105/90932024-09-27T22:24:30Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Lorente, Elena author Barriga, Alejandro author Barnea, Eilon author Mir-Gerrero, Carmen author Gebe, John A author Admon, Arie author Lopez, Daniel author 2016 Proper antiviral humoral and cellular immune responses require previous recognition of viral antigenic peptides that are bound to HLA class II molecules, which are exposed on the surface of antigen-presenting cells. The helper immune response is critical for the control and the clearance of human respiratory syncytial virus (HRSV) infection, a virus with severe health risk in infected pediatric, immunocompromised, and elderly populations. In this study, using a mass spectrometry analysis of complex HLA class II-bound peptide pools that were isolated from large amounts of HRSV-infected cells, 19 naturally processed HLA-DR ligands, most of them included in a complex nested set of peptides, were identified. Both the immunoprevalence and the immunodominance of the HLA class II response to HRSV were focused on one nonstructural (NS1) and two structural (matrix and mainly fusion) proteins of the infective virus. These findings have clear implications for analysis of the helper immune response as well as for antiviral vaccine design. Mol Cell Proteomics. 2016 Jun;15(6):2141-51. 10.1074/mcp.M115.057356 1535-9484 1535-9476 Molecular & cellular proteomics : MCP 27090790 http://hdl.handle.net/20.500.12105/9093 Structural and Nonstructural Viral Proteins Are Targets of T-Helper Immune Response against Human Respiratory Syncytial Virus