Summary
Respiratory syncytial virus (RSV) causes a substantial disease burden in infants and the elderly worldwide.Of the two glycoproteins present on the viral surface-the fusion protein (F) and the attachment protein (G)-only F is absolutely required for infection.RSV F is a class I fusion protein, which exists in a metastable conformation (prefusion F) that undergoes dramatic conformational changes to mediate viral entry.We isolated an antibody, called CR9501, that potently neutralizes RSV and prevents the rearrangements of prefusion F required for membrane fusion.Surprisingly, an RSV F-CR9501 complex crystallized as a monomer, despite being fused to a trimerization motif.Additional structural and biochemical studies demonstrated that CR9501 accelerates the disassembly of prefusion F trimers in
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