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dc.contributor.authorGonzález-Reyes, L
dc.contributor.authorRuiz-Argüello, M B
dc.contributor.authorGarcia-Barreno, Blanca 
dc.contributor.authorCalder, L
dc.contributor.authorLópez, J A
dc.contributor.authorAlbar, J P
dc.contributor.authorSkehel, J J
dc.contributor.authorWiley, D C
dc.contributor.authorMelero, Jose Antonio
dc.identifier.citationProc Natl Acad Sci U S A. 2001 Aug 14;98(17):9859-64es_ES
dc.description.abstractPreparations 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.es_ES
dc.description.sponsorshipWe are grateful to Rafael Blasco (Madrid) for the pRB21 plasmid and for the vRB12 vaccinia virus, and to Klaus-K. Conzelmann (Munich) for the BSR-T7/5 cells. This work was supported in part by Grants PM99–0014 from Ministerio de Ciencia y Tecnología and QLK2-CT-1999–00443 from the European Union (to J.A.M.), by the Medical Research Council (to J.J.S. and L.C.) and by the Howard Hughes Medical Institute. D.C.W. is an Investigator of the Howard Hughes Medical Institute. L.G.-R. was recipient of a predoctoral fellowship from Ministerio de Educación y Cultura (Spain) and M.B.R.-A. was recipient of a postdoctoral fellowship from the Comunidad de Madrid (Spain).es_ES
dc.publisherNational Academy of Scienceses_ES
dc.relation.isversionofPublisher's versiones_ES
dc.subject.meshAmino Acid Motifs es_ES
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAnimals es_ES
dc.subject.meshCell Line es_ES
dc.subject.meshCricetinae es_ES
dc.subject.meshCytopathogenic Effect, Viral es_ES
dc.subject.meshEndopeptidases es_ES
dc.subject.meshGiant Cells es_ES
dc.subject.meshHumans es_ES
dc.subject.meshKidney es_ES
dc.subject.meshMembrane Fusion es_ES
dc.subject.meshMesocricetus es_ES
dc.subject.meshMicroscopy, Electron es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshMutagenesis, Site-Directed es_ES
dc.subject.meshProtein Conformation es_ES
dc.subject.meshProtein Precursors es_ES
dc.subject.meshRecombinant Fusion Proteins es_ES
dc.subject.meshRespiratory Syncytial Viruses es_ES
dc.subject.meshStructure-Activity Relationship es_ES
dc.subject.meshViral Fusion Proteins es_ES
dc.subject.meshViral Proteins es_ES
dc.subject.meshProtein Processing, Post-Translationales_ES
dc.titleCleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusiones_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.contributor.funderMinisterio de Ciencia y Tecnología (España)es_ES
dc.contributor.funderEuropean Uniones_ES
dc.contributor.funderMedical Research Council (United Kingdom)es_ES
dc.contributor.funderHoward Hughes Medical Institutees_ES
dc.identifier.journalProceedings of the National Academy of Sciences of the United States of Americaes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES

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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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