Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids.
The low pH-dependent fusion of lipid membranes induced by two types of the fatty acylated influenza viral hemagglutinin has been studied by use of an energy transfer assay. When protein bound fatty acids were released from the hemagglutinin by hydroxylamine treatment viral fusion activity was inhibited. The extent of fusion inhibition correlates with the amount of fatty acids cleaved from the hemagglutinin. Virosomes prepared from fowl plague virus containing fatty acid free hemagglutinin showed a much lower fusion activity than control virosomes containing fatty acylated hemagglutinin. The hydroxylamine treatment applied has no detectable effects on the virus other than fatty acid release from its spike glycoproteins. These results support our previous hypothesis that protein bound fatty acids are involved in the induction of membrane fusion by the influenza hemagglutinin.
D000818:Animals; D002642:Chick Embryo; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D004735:Energy Transfer; D005227:Fatty Acids / Q000502:physiology*; D005347:Fibroblasts; D006389:Hemagglutinins, Viral; D006461:Hemolysis; D006863:Hydrogen-Ion Concentration; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007668:Kidney; D007700:Kinetics; D008561:Membrane Fusion; D009975:Orthomyxoviridae / Q000276:immunology*; D011485:Protein Binding
D005227:Fatty Acids; D006389:Hemagglutinins, Viral; D006898:Hydroxylamines; D019811:Hydroxylamine