Propagation of attenuated rubella virus strain HPV-77 in turkey embryo tissue culture. Brief report.
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In echo virus type 25/JV-4 the shut off of host cell protein synthesis took significantly longer and the kinetics of the synthesis of viral proteins and viral RNA occurred much later than in the poliovirus. However, these characteristics impaired neither polyprotein processing nor virus production in the JV-4 strain. In contrast the two wild strains M.1262 and Th.222 had a lower virus yield than strain JV-4. The presence of a high Mr protein in the pattern of viral proteins of wild strains suggested that a defect in the polyprotein processing was responsible for the decreased virus yield. The infectious cycle of strain Th.222 differed from that of strains JV-4 and M.1262 in the rapid inhibition of host cell translation and the extent of viral protein synthesis. The sensitivity to actinomycin D was also investigated. Strain M.1262 was found to be insensitive. The virus yield of strains JV-4 and Th.222 was three- and fourfold lower respectively in the presence of actinomycin D. This sensitivity to the antibiotic was observed during viral RNA synthesis in strain JV-4 and during viral protein synthesis in strain Th.222. These results suggest that cellular factors are involved in the replication of echo virus type 25 strains in MRC5 cells.
A virus isolated from the internal organs of a moribund corn snake (Elaphe guttata) replicated in reptilian cell cultures (IgH-2, TH-1 cells) between 10 and 30 degrees C. Highest infectivity titers of 10(5.5) TCID50/ml were obtained in IgH-2 cells at 25 degrees C. Infected IgH-2 cells showed the development of three morphologically different intranuclear inclusion bodies. During viral assembly the particles formed typical crystalline aggregates in the nucleus. About 64 h after infection progressive desintegration of the nuclear membrane was evident and virus particles were released into the cytoplasm. Different fish cell lines (CLC, CHSE-214, BF-2, PG, RTG-2) were not capable of propagating the virus. The DNA containing agent proved to be stable at pH3, more or less at pH 12 and to treatment with chloroform, but it was rapidly inactivated at 56 degrees C. Electron microscopy revealed nonenveloped icosahedral particles with a diameter of 65-70 nm.