Relationship of 2',3'-cyclic nucleotide 3'-phosphohydrolase activity of large enveloped RNA viruses to host cell activity.

Purified virions of the large RNA viruses show 2',3'-cyclic nucleotide 3'-phosphohydrolase (3'-CNPase) activity. The 3'-CNPase activity is virion-associated and stimulated by their treatment with nonionic detergents. Cytopathic viruses such as influenza A2 (Singapore/57), NDV, and VSV showed the specific activity of a virion-associated 3'-CNPase equal to or lower than the specific activity of host cell enzyme.

Localization of 2',3'-decycling phosphodiesterases in the Newcastle disease virus virion.

Purified Newcastle disease virus (NDV) virions possess 2',3'-cyclic nucleotide 2'-phosphohydrolase (2'-CNPase) and 2',3'-cyclic nucleotide 3'-phosphohydrolase (3'-CNPase) activities. These enzyme activities cannot be removed from the virion even after extensive purification by chromatography on controlled-pore glass. In the intact virion, the 3'-CNPase activity was stimulated by Triton X-100, while the 2'-CNPase activity was partially inhibited.

Cleavage of mouse ribosomal RNAs by the endonuclease associated with Newcastle disease virus.

Mouse ribosomal ribonucleic acids (rRNAs) are specifically cleaved to polynucleotides of lower molecular mass by the endonuclease associated with Newcastle disease virus (NDV). The 28 S RNA yielded a fragment of about Mr = 1.7 X 10(5) which is resistant to the endonuclease.

Polyacrylamide gel electrophoresis of the Kemerovo virus RNA.

Ribonuclease (RNase)-resistant RNA was isolated from partially purified Kemerovo virus by gel chromatography and or sucrose density gradient centrifugation. Double-stranded (ds) RNA only was found in the purified viral cores. The RNAs from both sources exhibited the same pattern of distribution in polyacrylamide gels.

Zonal density gradient electrophoresis of influenza A virus.

Enzymatic activities associated with influenza A virus purified by sedimentation in sucrose density gradient were removed from the virions by sucrose density gradient electrophoresis. A rapidly migrating electrophoretic fraction contained both structural viral polypeptides and chick embryo allantoic fluid polypeptides.