Characterization of some poliovirus temperature-sensitive mutants and poliovirus-related particle formation under nonpermissive conditions.
Investigation of 15 poliovirus temperature-sensitive (ts) mutants by using physiological tests [formation of virus-specific antigen and ribonucleic acid (RNA) under nonpermissive conditions] permitted us to divide them into three groups. From each group, one mutant was selected (ts 2, 5, 11), and a comparative study of poliovirus-related particle (5, 10, 73, and 150S) formation under permissive (36 C) and nonpermissive (40 C) conditions was carried out. The ts 2 and ts 11 are mutants with greatly reduced RNA synthesis which at 40 C produce particles with a sedimentation constant of 5S, and the ts 5 (RNA(+)) mutant produces both 5 and 10S particles. The relationship between different temperature-sensitive defects in the mutants is discussed. The results obtained indicate a possible role of 5S protein structures in morphogenesis of poliovirus.
D000327:Adsorption; D000596:Amino Acids / Q000378:metabolism; D000941:Antigens / Q000378:metabolism; D002247:Carbon Isotopes; D002499:Centrifugation, Density Gradient; D005455:Fluorescent Antibody Technique; D005827:Genetics, Microbial; D006367:HeLa Cells; D009154:Mutation; D017955:Poliovirus / Q000254:growth & development* / Q000276:immunology / Q000378:metabolism / Q000472:pathogenicity; D011492:Protein Hydrolysates / Q000378:metabolism; D012367:RNA, Viral / Q000096:biosynthesis; D013053:Spectrophotometry; D013395:Sucrose; D013696:Temperature; D014529:Uridine / Q000378:metabolism; D014764:Viral Proteins / Q000096:biosynthesis; D014779:Virus Replication
D000596:Amino Acids; D000941:Antigens; D002247:Carbon Isotopes; D011492:Protein Hydrolysates; D012367:RNA, Viral; D014764:Viral Proteins; D013395:Sucrose; D014529:Uridine