期刊
NATURE STRUCTURAL BIOLOGY
卷 10, 期 12, 页码 1048-1053出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb1012
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Formation of helix bundles has been proposed as a general mechanism for viral and cellular membrane fusion reactions. Class I viral fusion proteins, including HIV Env and influenza hemagglutinin (HA), form six-helix bundles in their fusogenic forms. The HIV Env six-helix bundle extends to the membrane proximal end of the protein, where it is poised to pull the fusing membranes together. In contrast, the HA six-helix bundle is located at the membrane distal end of the protein. It is followed by a C-terminal leash that packs into the grooves and extends to the membrane proximal end of the coiled--coil. Here, we describe the ability of C-terminal leash mutants to change conformation and induce fusion. Our data indicate that packing of the C-terminal leash into the grooves of the coiled-coil is necessary for HA to mediate the lipid mixing stage of fusion, and that hydrophobic membrane proximal leash residues secure this interaction. Therefore, HA employs a leash in the groove, rather than a helix-bundle, mechanism of membrane fusion.
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