Machupo virus polypeptides: identification by immunoprecipitation.
The most abundant protein in purified Machupo virions (Corvallo strain) labelled with 14C-Protein hydrolysate is a 64 K polypeptide which is associated with virion RNAs. Another structural polypeptide, 37 K, solubilized by nonionic detergent seems to be a major surface glycoprotein. In addition to this, a 78 K polypeptide and a minor 50 K polypeptide have been detected. In Machupo virus infected cells three virus-specific polypeptides similar in size to those described for structural polypeptides were immunoprecipitated with anti-Machupo virus serum. The most abundant virus-specific polypeptide was nonglycosylated (64 K, NP), and the others were glycosylated polypeptides (78 K and 37 K). The synthesis of NP and 78 K polypeptides was recognized at the beginning of a log phase of virus replication. Pulse-chase experiments as well as experiments with an arginine analogue, canavanine (to block proteolytic processing) suggest that 78 K is a precursor for structural glycoproteins of Machupo virions.
D000818:Animals; D001116:Arenaviridae / Q000032:analysis*; D006477:Arenaviruses, New World / Q000032:analysis*; D002172:Canavanine / Q000494:pharmacology; D002460:Cell Line; D011232:Chemical Precipitation; D006224:Cricetinae; D005944:Glucosamine / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis* / Q000276:immunology; D014316:Tritium; D014764:Viral Proteins / Q000032:analysis* / Q000096:biosynthesis / Q000276:immunology; D014771:Virion / Q000032:analysis
D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins; D014316:Tritium; D002172:Canavanine; D005944:Glucosamine