Effects of altering palmitylation sites on biosynthesis and function of the influenza virus hemagglutinin.
Mutagenesis studies indicated that the three cytoplasmic cysteines of the influenza virus A/Japan/305/57 hemagglutinin (HA) are all palmitylated, but to an unequal extent. Replacement of all three cysteines abolished palmitylation, but affected neither HA biosynthesis nor function. Palmitate was not required for HA to be incorporated into virions.
Naim
H Y
HY
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235-9038.
Amarneh
B
B
Ktistakis
N T
NT
Roth
M G
MG
D000595:Amino Acid Sequence; D000818:Animals; D002459:Cell Fusion; D002460:Cell Line; D003545:Cysteine; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000096:biosynthesis* / Q000235:genetics; D009980:Influenza A virus / Q000235:genetics* / Q000276:immunology; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000096:biosynthesis* / Q000235:genetics
D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D010169:Palmitic Acids; D014759:Viral Envelope Proteins; D019308:Palmitic Acid; D014357:Trypsin; D003545:Cysteine