González-Reyes, LRuiz-Argüello, M BGarcia-Barreno, BlancaCalder, LLópez, J AAlbar, Juan PabloSkehel, J JWiley, D CMelero, Jose Antonio2020-05-072020-05-072001-08-14Proc Natl Acad Sci USA. 2001 Aug 14;98(17):9859-64.0027-8424http://hdl.handle.net/20.500.12105/9952Preparations of purified full-length fusion (F) protein of human respiratory syncytial virus (HRSV) expressed in recombinant vaccinia-F infected cells, or of an anchorless mutant (F(TM(-))) lacking the C-terminal 50 amino acids secreted from vaccinia-F(TM(-))-infected cells contain a minor polypeptide that is an intermediate product of proteolytic processing of the F protein precursor F0. N-terminal sequencing of the intermediate demonstrated that it is generated by cleavage at a furin-motif, residues 106-109 of the F sequence. By contrast, the F1 N terminus derives from cleavage at residue 137 of F0 which is also C-terminal to a furin recognition site at residues 131-136. Site-directed mutagenesis indicates that processing of F0 protein involves independent cleavage at both sites. Both cleavages are required for the F protein to be active in membrane fusion as judged by syncytia formation, and they allow changes in F structure from cone- to lollipop-shaped spikes and the formation of rosettes by anchorless F.engVoRhttp://creativecommons.org/licenses/by-nc-sa/4.0/Amino Acid MotifsAmino Acid SequenceAnimalsCell LineCricetinaeCytopathogenic Effect, ViralEndopeptidasesGiant CellsHumansKidneyMembrane FusionMesocricetusMicroscopy, ElectronMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationProtein PrecursorsRecombinant Fusion ProteinsRespiratory Syncytial VirusesStructure-Activity RelationshipViral Fusion ProteinsViral ProteinsProtein Processing, Post-TranslationalAtribución-NoComercial-CompartirIgual 4.0 Internacional1149367598179859-6410.1073/pnas.151098198Proceedings of the National Academy of Sciences of the United States of Americaopen access