2026-08-29T12:39:55Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/104162024-09-27T20:20:31Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609

00925njm 22002777a 4500 dc Rossey, Iebe author Gilman, Morgan S A author Kabeche, Stephanie C author Sedeyn, Koen author Wrapp, Daniel author Kanekiyo, Masaru author Chen, Man author Spitaels, Jan author Graham, Barney S author Schepens, Bert author McLellan, Jason S author Saelens, Xavier author Mas-Lloret, Vicente author Melero, Jose Antonio author 2017 Human respiratory syncytial virus (RSV) is the main cause of lower respiratory tract infections in young children. The RSV fusion protein (F) is highly conserved and is the only viral membrane protein that is essential for infection. The prefusion conformation of RSV F is considered the most relevant target for antiviral strategies because it is the fusion-competent form of the protein and the primary target of neutralizing activity present in human serum. Here, we describe two llama-derived single-domain antibodies (VHHs) that have potent RSV-neutralizing activity and bind selectively to prefusion RSV F with picomolar affinity. Crystal structures of these VHHs in complex with prefusion F show that they recognize a conserved cavity formed by two F protomers. In addition, the VHHs prevent RSV replication and lung infiltration of inflammatory monocytes and T cells in RSV-challenged mice. These prefusion F-specific VHHs represent promising antiviral agents against RSV. Nat Commun . 2017 Feb 13;8:14158. 10.1038/ncomms14158 2041-1723 Nature communications 28194013 http://hdl.handle.net/20.500.12105/10416 Potent single-domain antibodies that arrest respiratory syncytial virus fusion protein in its prefusion state.