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Begoña Ruiz-Argüello, M.; González-Reyes, Luis; Calder, Leslie J.; Palomo, Concepción; Martı́n, Diana; Saı́z, Marı́a J.; Garcı́a-Barreno, Blanca; Skehel, John J.; Melero, José A.
Virology (New York, N.Y.), 07/2002, Letnik: 298, Številka: 2Journal Article
We have examined the consequences of cleaving the fusion glycoprotein (F) of human respiratory syncytial virus (HRSV) at two distinct furin-recognition sites. Purified anchorless F is a mixture of unaggregated cone-shaped molecules and rosettes of lollipop-shaped spikes. The unaggregated molecules contain a proportion of uncleaved F0 and an intermediate, FΔ1–109, cleaved only at site I, residues 106–109. Inhibition of cleavage at site I, by two amino acid changes (R108N/R109N), reduces the proportion of aggregated molecules with a concomitant increase in the amount of unprocessed F0. Inhibition of cleavage at site II, residues 131–136, by deletion of four amino acids (Δ131–134), abrogates aggregation of anchorless F and all molecules are seen as individual cone-shaped rods. In vitro cleavage of anchorless F, or mutant Δ131–134, with trypsin at 4, 20, or 37°C, under conditions in which cleavage at site II is complete in all molecules, leads to their aggregation in rosettes of lollipop-shaped spikes. Thus, cleavage at site II is required for the structural changes in anchorless F that lead to changes in shape and to aggregation. The segment between sites I and II, residues 110–136, is not associated with anchorless F in the supernatant of infected cell cultures, indicating that it is released from the processed protein when cleavage at sites I and II is completed.
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