title: Suppression of glycoprotein formation of Semliki Forest, influenza, and avian sarcoma virus by tunicamycin.
abstract: Tunicamycin, a new antibiotic, halts the formation of physical particles of Semliki forest and fowl plague virus, whereas avian oncornavirus particles which show a reduction in infectivity and do not contain detectable labeled glycoprotein are released in the presence of the drug. In Semliki forest virus-infected cells only the protein moieties of the glycoproteins could be labeled. In cells infected with fowl plague and avian sarcoma virus neither intact glycoproteins nor their protein moieties could be detected. By using a protease inhibitor (N-alpha-p-tosyl-L-lysin chloromethyl ketone, TLCK) it could be shown, however, that the carbohydrate-free hemagglutinin precursor of influenza virus is synthesized but is presumably degraded by intracellular proteases in the absence of TLCK as a consequence of the lack of carbohydrate.
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001358:Avian Sarcoma Viruses / Q000187:drug effects* / Q000378:metabolism; D002642:Chick Embryo; D046508:Culture Techniques; D005944:Glucosamine / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology; D006023:Glycoproteins / Q000096:biosynthesis*; D006389:Hemagglutinins, Viral / Q000032:analysis; D009980:Influenza A virus / Q000187:drug effects* / Q000378:metabolism; D008358:Mannose / Q000378:metabolism; D012672:Semliki forest virus / Q000187:drug effects* / Q000378:metabolism; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014764:Viral Proteins / Q000096:biosynthesis*
chemical_list: D000900:Anti-Bacterial Agents; D006023:Glycoproteins; D006389:Hemagglutinins, Viral; D014764:Viral Proteins; D014107:Tosyllysine Chloromethyl Ketone; D005944:Glucosamine; D008358:Mannose