Ultrastructural studies of H-1 parvovirus replication. IV. Crystal development and structure with the temperature-sensitive mutant ts1.
Electron microscopy was used to study the development and structure of viral crystals of ts1, a temperature-sensitive mutant of H-1 parvovirus. At early times postinfection, at the restrictive temperature, empty H-1 capsids aggregated to form conspicuous noncrystalline conglomerates in human NB cell nuclei; these particles did not associate with euchromatin as in wild-type H-1 infections. Later on, the capsid aggregated appeared to form polycrystals exhibiting rod-like, hexagonal, and cubic patterns that were interconvertible using a goniometer specimen stage. The unit cell of this crystal was cubic, consisted of 16 empty particles, and measured 50 nm on each side. Full particles made at the permissive temperature were never observed under restrictive conditions. Experiments in which cultures were shifted form the permissive to the restrictive temperature showed that full virions were not incorporated into crystals. The crystals dissociated into individual particles when changes were made from restrictive to permissive conditions. Correlations between the formation of crystals at the restrictive temperature, their dissociation into capsid components after shifting from the restrictive to the permissive state, and the extent of host cell damage were also observed. Possible roles of cellular functions in regulating ts1 H-1 polycrystal assembly and dissociation are discussed.
D002213:Capsid; D002467:Cell Nucleus / Q000382:microbiology; D003461:Crystallography; D007181:Inclusion Bodies, Viral; D009024:Morphogenesis; D009154:Mutation; D010321:Parvoviridae / Q000235:genetics / Q000254:growth & development* / Q000648:ultrastructure; D013696:Temperature; D014779:Virus Replication