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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.
Proceedings of the National Academy of Sciences, 08/2001, Letnik: 98, Številka: 17Journal Article
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 (FTM-) lacking the C-terminal 50 amino acids secreted from vaccinia-FTM--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.
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