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dc.contributor.author | González-Reyes, L | |
dc.contributor.author | Ruiz-Argüello, M B | |
dc.contributor.author | Garcia-Barreno, Blanca | |
dc.contributor.author | Calder, L | |
dc.contributor.author | López, J A | |
dc.contributor.author | Albar, Juan Pablo | |
dc.contributor.author | Skehel, J J | |
dc.contributor.author | Wiley, D C | |
dc.contributor.author | Melero, Jose Antonio | |
dc.date.accessioned | 2020-05-07T12:36:37Z | |
dc.date.available | 2020-05-07T12:36:37Z | |
dc.date.issued | 2001-08-14 | |
dc.identifier.citation | Proc Natl Acad Sci USA. 2001 Aug 14;98(17):9859-64. | es_ES |
dc.identifier.issn | 0027-8424 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/9952 | |
dc.description.abstract | Preparations 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.sponsorship | We 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.language.iso | eng | es_ES |
dc.publisher | National Academy of Sciences | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject.mesh | Amino Acid Motifs | es_ES |
dc.subject.mesh | Amino Acid Sequence | es_ES |
dc.subject.mesh | Animals | es_ES |
dc.subject.mesh | Cell Line | es_ES |
dc.subject.mesh | Cricetinae | es_ES |
dc.subject.mesh | Cytopathogenic Effect, Viral | es_ES |
dc.subject.mesh | Endopeptidases | es_ES |
dc.subject.mesh | Giant Cells | es_ES |
dc.subject.mesh | Humans | es_ES |
dc.subject.mesh | Kidney | es_ES |
dc.subject.mesh | Membrane Fusion | es_ES |
dc.subject.mesh | Mesocricetus | es_ES |
dc.subject.mesh | Microscopy, Electron | es_ES |
dc.subject.mesh | Molecular Sequence Data | es_ES |
dc.subject.mesh | Mutagenesis, Site-Directed | es_ES |
dc.subject.mesh | Protein Conformation | es_ES |
dc.subject.mesh | Protein Precursors | es_ES |
dc.subject.mesh | Recombinant Fusion Proteins | es_ES |
dc.subject.mesh | Respiratory Syncytial Viruses | es_ES |
dc.subject.mesh | Structure-Activity Relationship | es_ES |
dc.subject.mesh | Viral Fusion Proteins | es_ES |
dc.subject.mesh | Viral Proteins | es_ES |
dc.subject.mesh | Protein Processing, Post-Translational | es_ES |
dc.title | Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución-NoComercial-CompartirIgual 4.0 Internacional | * |
dc.identifier.pubmedID | 11493675 | es_ES |
dc.format.volume | 98 | es_ES |
dc.format.number | 17 | es_ES |
dc.format.page | 9859-64 | es_ES |
dc.identifier.doi | 10.1073/pnas.151098198 | es_ES |
dc.contributor.funder | Ministerio de Ciencia y Tecnología (España) | |
dc.contributor.funder | Unión Europea | |
dc.contributor.funder | Medical Research Council (Reino Unido) | |
dc.contributor.funder | Howard Hughes Medical Institute | |
dc.description.peerreviewed | Sí | es_ES |
dc.relation.publisherversion | https://doi.org/10.1073/pnas.151098198 | es_ES |
dc.identifier.journal | Proceedings of the National Academy of Sciences of the United States of America | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/PM99–0014 | es_ES |
dc.relation.projectID | info:eu_repo/grantAgreement/ES/QLK2-CT-1999–00443 | es_ES |
dc.rights.accessRights | open access | es_ES |