title: Different palmitoylation of paramyxovirus glycoproteins.
abstract: 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.
authors.affiliation: Institut für Virologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
authors.forename: M
authors.initials: M
authors.lastname: Veit
authors.forename: M F
authors.initials: MF
authors.lastname: Schmidt
authors.forename: R
authors.initials: R
authors.lastname: Rott
mesh_terms: 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
chemical_list: D005227:Fatty Acids; D006023:Glycoproteins; D010169:Palmitic Acids; D014764:Viral Proteins; D015678:Viral Structural Proteins