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. 1981 Aug;39(2):432–437. doi: 10.1128/jvi.39.2.432-437.1981

Stable association of viral protein VP1 with simian virus 40 DNA.

J N Brady, C A Lavialle, M F Radonovich, N P Salzman
PMCID: PMC171352  PMID: 6168774

Abstract

Mild dissociation of simian virus 40 particles releases a 110S virion core nucleoprotein complex containing histones and the three viral proteins VP1, VP2, and VP3. The association of viral protein VP1 within this nucleoprotein complex is mediated at least partially through a strong interaction with the viral DNA. Treatment of the virion-derived 110S nucleoprotein complex with 0.25% Sarkosyl dissociated VP2, VP3, and histones, leaving a stable VP1-DNA complex. The VP1-DNA complex had a sedimentation value of 30S and a density of 1.460 g/cm3. The calculated molecular weight of the complex was 7.9 x 10(6), with an average of 100 VP1 molecules per DNA. Agarose gel electrophoresis of the VP1-DNA complex demonstrated that VP1 is associated not only with form I and form II simian virus 40 DNAs but also with form III simian virus 40 DNA generated by cleavage with EcoRI.

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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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