Uncoating-like modification of poliovirus capsid resulting from the cooperative effects of subfreezing temperature and submolar concentrations of urea.
Inactivation of poliovirus at subfreezing temperature in the presence of unusually low concentrations of urea (less than or equal to 0.5 M) was investigated. Whereas serotypes 1 and 2 are very sensitive, type 3 is resistant. Inactivation cannot be attributed to concentration of solutes since temperature must be reduced below -13 degrees C for loss of infectivity. Characteristics of the inactivated virion are similar to those of virions in the early stages of uncoating in HeLa cells, viz., loss of infectivity, sensitivity to proteases and detergents, change in isoelectric point, retention of intact genome, and in some instances, loss of VP4. The molecular basis for inactivation is considered to be dissociation of water bound to capsid proteins thereby causing irreversible denaturation of native tertiary structure. The results of this study are discussed in terms of their relevance to the early stages of uncoating in vivo.
D000327:Adsorption; D002213:Capsid; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000494:pharmacology; D005615:Freezing; D005814:Genes, Viral; D007526:Isoelectric Point; D046911:Macromolecular Substances; D017955:Poliovirus / Q000032:analysis / Q000254:growth & development*; D014508:Urea; D014764:Viral Proteins; D014867:Water
D046911:Macromolecular Substances; D014764:Viral Proteins; D014867:Water; D014508:Urea; D002918:Chymotrypsin