Structural and physiological properties of mengovirus: avirulent, hemagglutination-defective mutants express altered alpha (1 D) proteins and are adsorption-defective.
Structural and physiological properties of two mutants of mengovirus, 205 and 280, were compared to those of wild-type virus to understand the molecular basis of changes exhibited in their biological function. Two dimensional gel electrophoresis of wild-type and mutant structural proteins revealed alterations in the isoelectric character of the alpha (1 D) protein of both mutant 205 and 280. These data suggest that alterations in the alpha (1 D) protein may be responsible for the phenotypic changes by the mutants. A delay in detectable virus-specified protein synthesis was exhibited in mutant-infected cells in comparison to wild-type. The amount of RNA synthesized in mutant- and revertant-infected cells was less than that synthesized in wild-type infected cells. Changes in virus-specified macromolecular synthesis in mutant and revertant-infected cells reflected a decrease in the ability of the viruses to attach to cells.
D000818:Animals; D002448:Cell Adhesion; D002460:Cell Line; D006224:Cricetinae; D006389:Hemagglutinins, Viral / Q000032:analysis; D007526:Isoelectric Point; D008574:Mengovirus / Q000032:analysis / Q000502:physiology*; D008970:Molecular Weight; D009154:Mutation; D010446:Peptide Fragments / Q000032:analysis; D012367:RNA, Viral / Q000096:biosynthesis; D014764:Viral Proteins / Q000032:analysis* / Q000096:biosynthesis / Q000235:genetics
D006389:Hemagglutinins, Viral; D010446:Peptide Fragments; D012367:RNA, Viral; D014764:Viral Proteins