Intermediates in influenza induced membrane fusion.

摘要: Our results show that the mechanism by which influenza virus fuses with target membranes involves sequential complex changes in hemagglutinin (HA, viral fusion protein) and contact site between membrane. To render individual steps amenable to study, we worked at 0 degree C decreased rate of increased efficiency. The 37 degrees was similar. process began a conformational change HA exposed peptides but did not lead dissociation tops ectodomain trimer. protein led immediate hydrophobic attachment liposomes. Attachment followed lag period (4-8 min C, 0.6-2 s C) during rearrangements occurred membrane liposome. After further series final bilayer merger took place. This event pH dependent. At efficient without top domains trimer, suggesting transient conformation is responsible for physiological temperatures. observations revised model mediated fusion.