An assembly defect as a result of an attenuating mutation in the capsid proteins of the poliovirus type 3 vaccine strain

J Virol. 1991 Oct;65(10):5225-31. doi: 10.1128/JVI.65.10.5225-5231.1991.

Abstract

The molecular basis of the temperature-sensitive (ts) phenotype of P3/Sabin, the type 3 vaccine strain of poliovirus, was investigated in light of the known correlation between ts and attenuation phenotypes. A phenylalanine at residue 91 of the capsid protein VP3 was a major determinant of both phenotypes, and attenuation and ts could be reverted by the same second-site mutations. The ts phenotype was due to a defect early in the assembly process that inhibited the formation of 14S pentamers, empty capsids, and virions. It was further shown that capsid proteins that were not incorporated into higher-order structures had short half-lives at the nonpermissive temperature.

MeSH terms

  • Capsid / genetics*
  • Capsid / immunology
  • Capsid / isolation & purification
  • Cell Line
  • Centrifugation, Density Gradient
  • Humans
  • Kinetics
  • Mutation*
  • Phenotype
  • Poliovirus / genetics*
  • Poliovirus / growth & development
  • Poliovirus / immunology
  • Poliovirus Vaccine, Oral*
  • RNA, Viral / genetics
  • RNA, Viral / isolation & purification
  • Temperature
  • Vaccines, Attenuated*

Substances

  • Poliovirus Vaccine, Oral
  • RNA, Viral
  • Vaccines, Attenuated