Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties.
The effects of deacylating the H3 influenza hemagglutinin (HA) on its membrane fusion activity were investigated. Chemical deacylation caused no change in the ability of HA to fuse liposomes in vitro. Site-specific mutagenesis of the three cysteine residues in the cytoplasmic tail singly, or in combination, showed that all three were palmitoylated. Substitution of one, two, or all three cysteines with serine and subsequent lack of palmitoylation at mutated sites had no effect on the pH of the conformational change in HA required for fusion activity or the extent of fusion activity.
Steinhauer
D A
DA
National Institute for Medical Research, Mill Hill, London, United Kingdom.
Wharton
S A
SA
Wiley
D C
DC
Skehel
J J
JJ
D000215:Acylation; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000235:genetics / Q000378:metabolism*; D009980:Influenza A virus / Q000235:genetics / Q000502:physiology*; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010169:Palmitic Acids / Q000032:analysis; D011487:Protein Conformation; D014162:Transfection; D014616:Vaccinia virus / Q000235:genetics; D014759:Viral Envelope Proteins / Q000378:metabolism*
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010169:Palmitic Acids; D014759:Viral Envelope Proteins