Different palmitoylation of paramyxovirus glycoproteins.
Different paramyxoviruses were analyzed for the covalent attachment of fatty acids into their structural proteins. The fusion protein (F) of Newcastle diseases virus and the hemagglutinin-neuraminidase (HN) of Simian virus 5 are fatty acylated, whereas the glycoproteins of Sendai virus are fatty acid free. The fatty acid linkage is labile to treatment with hydroxylamine. SDS-PAGE in the presence of mercaptoethanol releases some of the covalently bound acyl chains.
Veit
M
M
Institut für Virologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
Schmidt
M F
MF
Rott
R
R
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005227:Fatty Acids / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009522:Newcastle disease virus / Q000378:metabolism; D010169:Palmitic Acids / Q000378:metabolism*; D010222:Parainfluenza Virus 1, Human / Q000378:metabolism; D010252:Paramyxoviridae / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*; D015678:Viral Structural Proteins
D005227:Fatty Acids; D006023:Glycoproteins; D010169:Palmitic Acids; D014764:Viral Proteins; D015678:Viral Structural Proteins