title: Intracellular posttranslational modifications of S1133 avian reovirus proteins.
abstract: Avian reovirus S1133 specifies at least 10 primary translation products, eight of which are present in the viral particle and two of which are nonstructural proteins. In the work presented here, we studied the covalent modifications undergone by these translation products in the infected cell. The structural polypeptide mu2 was shown to be intracellularly modified by both myristoylation and proteolysis. The site-specific cleavage of mu2 yielded a large carboxy-terminal fragment and a myristoylated approximately 5,500-Mr peptide corresponding to the amino terminus. Both mu2 and its cleavage products were found to be structural components of the reovirion. Most avian reovirus proteins were found to be glycosylated and to have a blocking group at the amino terminus. In contrast to the mammalian reovirus system, none of the avian reovirus polypeptides was found to incorporate phosphorus during infection. Our results add to current understanding of the similarities and differences between avian and mammalian reoviruses.
authors.affiliation: Departamento de Bioquímica y Biologia Molecular, Facultad de Farmacia, Santiago de Compostela, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Varela
authors.forename: J
authors.initials: J
authors.lastname: Martínez-Costas
authors.forename: M
authors.initials: M
authors.lastname: Mallo
authors.forename: J
authors.initials: J
authors.lastname: Benavente
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts; D008715:Methionine / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism; D018165:Orthoreovirus / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D010449:Peptide Mapping; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013462:Sulfur Radioisotopes; D014764:Viral Proteins / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000096:biosynthesis / Q000378:metabolism
chemical_list: D009227:Myristic Acids; D010446:Peptide Fragments; D013462:Sulfur Radioisotopes; D014764:Viral Proteins; D015678:Viral Structural Proteins; D019814:Myristic Acid; D008715:Methionine