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. 1969 Aug;4(2):141–146. doi: 10.1128/jvi.4.2.141-146.1969

Fate of Sendai Virus Ribonucleoprotein in Virus-infected Cells

A G Bukrinskaya 1, V M Zhdanov 1, G K Vorkunova 1
PMCID: PMC375848  PMID: 4308913

Abstract

The cytoplasmic extracts of Ehrlich ascites tumor cells infected with 32PO4 and 3H-leucine-labeled Sendai virus have been examined during the course of infection with respect to sedimentation behavior and buoyant densities of input virus radioactivity. It was found that 32P and 3H radioactivities were coincident, and, at 30 min after infection, the bulk of radioactivity was recovered in the polysome region of a sucrose gradient in the position of Sendai virus ribonucleoprotein (210S). The heterogeneity of radioactivity profiles appeared at 1 hr after infection and increased during 6 hr of incubation. The buoyant densities of input virus components were determined by banding in CsCl gradient. Here again the bulk of coincident 32P and 3H radioactivity at 30 min after infection banded at the same density as Sendai virus ribonucleoprotein (1.31 g/cm3.) This component disappeared at 3 hr after infection, and 32P and 3H radioactivities were now found in components banded at densities 1.38, 1.41, 1.45, 1.49, and 1.55 g/cm3. The results presented are consistent with the idea that virus ribonucleoprotein is retained in the cytoplasm of infected cells during at least 6 hr of incubation, being partly deproteinized in the course of infection. The nature of components which banded at ρ = 1.41, 1.45, 1.49, and 1.55 as complexes of partly deproteinized ribonucleoprotein with ribosomes will be described in a separate paper.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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