Defective mutant of Sindbis virus with a smaller-molecular-weight form of the E1 glycoprotein.
We have isolated from a single plaque a mutant of Sindbis virus characterized by an E1 glycoprotein with higher electrophoretic mobility. This higher mobility is not attributable to a different extent of glycosylation of the protein nor to an altered proteolytic maturation pathway of the polypeptide precursor, but is the result of a deletion occurring during the replication of the viral RNA. The 26S RNA (the messenger for the Sindbis structural proteins) extracted from cells infected with the mutant is about 0.75 x 10(5) daltons smaller than the 26S RNA from the parental strain. As a consequence, in cells infected with the mutant, an E1 glycoprotein is synthesized with a polypeptide chain about 70 amino acids shorter. The biological relevance of this naturally occurring deletion of the viral genome is discussed.
D003673:Defective Viruses / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D006023:Glycoproteins / Q000235:genetics*; D008970:Molecular Weight; D009154:Mutation; D012333:RNA, Messenger / Q000235:genetics; D012367:RNA, Viral / Q000235:genetics; D012845:Sindbis Virus / Q000235:genetics* / Q000378:metabolism; D014415:Tunicamycin / Q000494:pharmacology; D014764:Viral Proteins / Q000235:genetics*
D006023:Glycoproteins; D012333:RNA, Messenger; D012367:RNA, Viral; D014764:Viral Proteins; D014415:Tunicamycin