Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement.

Abstract excerpt

For influenza virus hemagglutinin, an N-cap structure, created at low pH, interacts with membrane-proximal residues (173-178), bringing fusion peptides and membrane-spanning domains close together. Mutational analysis was used to define the role of these interactions in membrane fusion. For all N-cap mutants, both lipid and aqueous dye spread was greatly reduced. Mutation at residues that interact with the N-cap...

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