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Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion

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Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion
Id. 17628265
Idioma inglés
Titulo Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion
Autor(es) González-Reyes, Luis
Ruiz-Argüello, M. Begoña
García-Barreno, Blanca
Calder, Leslie
López, Juan A.
Albar, Juan P.
Skehel, John J.
Wiley, Don C.
Melero, José A.
Localización http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=55543
Versión 1.0
Estado Final
Descripción 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 (FTMâ??) lacking the C-terminal 50 amino acids secreted from vaccinia-FTMâ??-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 106â??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 131â??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.
Palabras clave Biological Sciences
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Copyright © 2001, The National Academy of Sciences
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Fecha de contribución 08-feb-2008
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