Relationship of 2',3'-cyclic nucleotide 3'-phosphohydrolase activity of large enveloped RNA viruses to host cell activity
Jazyk angličtina Země Švýcarsko Médium print
Typ dokumentu časopisecké články
PubMed
1688073
Knihovny.cz E-zdroje
- MeSH
- 2',3'-cyklická nukleotid 3'-fosfodiesteráza MeSH
- 2',3'-cyklické nukleotidfosfodiesterasy fyziologie MeSH
- buněčné linie MeSH
- fosfodiesterasy * MeSH
- Orthomyxoviridae enzymologie MeSH
- replikace viru fyziologie MeSH
- Retroviridae enzymologie MeSH
- RNA-viry enzymologie fyziologie MeSH
- virus newcastleské nemoci enzymologie MeSH
- virus vezikulární stomatitidy, kmen Indiana enzymologie MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 2',3'-cyklická nukleotid 3'-fosfodiesteráza MeSH
- 2',3'-cyklické nukleotidfosfodiesterasy MeSH
- fosfodiesterasy * MeSH
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. Retroviruses are an example of extreme relationship of 3'-CNPase to virion. With the AMV-BAI-A associated enzyme activity increased after Triton X-100 treatment ten times more than that associated with other viruses examined. The specific activity of virus-associated 3'-CNPase was 16-28 times higher than that in chick myeloblasts. BLV showed a very low enzyme activity. The correlation between the activity of cellular 3'-CNPase and virus yield showed that 3'-CNPase could belong to cellular factors influencing virus replication.
