title: Fatty acylation of rabies virus proteins.
abstract: The fatty acylation of rabies virus (CVS strain) proteins was investigated. [3H]palmitic acid was found to be incorporated into the glycoprotein G and to a lesser extent into the membrane-associated protein M2. The fatty acid linkage on G was sensitive to sodium borohydride, mercaptoethanol, and hydroxylamine, indicating that the linkage was of the thiolester type. Bromelain digestion indicated that the palmitoylation site on G was located in the intracytoplasmic domain or in the transmembrane domain in which there is only one cysteine in position 461. Therefore, palmitoylation is likely to occur at this position. In the case of M2, the linkage was also sensitive to hydroxylamine and sodium borohydride and to a lesser extent to mercaptoethanol, suggesting that the linkage also occurred on a cysteine.
authors.affiliation: Laboratoire de Génétique des Virus, CNRS, Gif sur Yvette Cedex, France.
authors.forename: Y
authors.initials: Y
authors.lastname: Gaudin
authors.forename: C
authors.initials: C
authors.lastname: Tuffereau
authors.forename: A
authors.initials: A
authors.lastname: Benmansour
authors.forename: A
authors.initials: A
authors.lastname: Flamand
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D007700:Kinetics; D008969:Molecular Sequence Data; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D011820:Rabies virus / Q000378:metabolism*; D013045:Species Specificity; D014763:Viral Matrix Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D010169:Palmitic Acids; D014763:Viral Matrix Proteins; D014764:Viral Proteins; D019308:Palmitic Acid