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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, F Δ1–109 , cleaved only at site I,...
Full-length fusion (F) glycoprotein of human respiratory syncytial virus (HRSV) and a truncated anchorless mutant lacking the C-terminal 50 amino acids were expressed from vaccinia recombinants and purified by immunoaffinity chromatography and sucrose gradient centrifugation. Electron microscopy of full-length F protein in the absence of detergents revealed micelles, (i.e., rosettes) containing two...
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