Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions.
AUTOR(ES)
Compton, S R
RESUMO
A temperature-sensitive mutant of poliovirus, VP2-103, was isolated and characterized. A single nucleotide change, resulting in the substitution of glutamine for arginine at amino acid 76 of the capsid protein VP2, prevented the maturation of virions at the nonpermissive temperature. Particles indistinguishable from the previously elusive provirions were observed; these particles have been proposed to be penultimate in virion morphogenesis. Cleavage of VP0 into VP2 and VP4, the products found in mature virions, was not observed in VP2-103-infected cells at the nonpermissive temperature. The cleavage of VP0 in wild-type poliovirus-infected cells is dependent on RNA packaging; this reaction has been postulated to be autocatalytic. The existence of RNA-containing provirionlike particles in VP2-103-infected cells shows that RNA packaging can be uncoupled from VP0 cleavage.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=247868Documentos Relacionados
- Poliovirus Mutants at Histidine 195 of VP2 Do Not Cleave VP0 into VP2 and VP4
- Temperature-Sensitive Mutant of Bacillus subtilis That Accumulates Membrane-Associated Protein Inclusions
- Rescue of Temperature-sensitive Poliovirus 1
- Temperature-Sensitive Behavior of the Hemagglutinin in a Temperature-Sensitive Mutant Virion of Sindbis 1
- Temperature-sensitive Escherichia coli mutant producing a temperature-sensitive sigma subunit of DNA-dependent RNA polymerase.
