6533b872fe1ef96bd12d38f9
RESEARCH PRODUCT
In vitro reconstitution of rotavirus transcriptional activity using viral cores and recombinant baculovirus expressed VP 6
Jean CohenPierre PothierAna María SandinoGwenola TosserEvelyne KohliE. Spencersubject
RotaviruspolypeptidereplicationTranscription Genetic[SDV]Life Sciences [q-bio]virusesReoviridaeimmunogenicitymedicine.disease_causeViruslaw.inventionCapsidsingle-shelled particlelawVirologyRotavirusGene expressionmedicinebovine rotavirusAntigens ViralPolymerasebiologyViral Core Proteinsvirus diseasesDNA-Directed RNA PolymerasesGeneral Medicinebiology.organism_classificationNucleotidyltransferaseVirologyMolecular biologyRecombinant ProteinsIn vitro[SDV] Life Sciences [q-bio]biology.proteinRecombinant DNACapsid ProteinsElectrophoresis Polyacrylamide GelproteinBaculoviridaedescription
International audience; Purified baculovirus-expressed group A rotavirus VP6 polypeptide was shown to be active in the recovery of the transcriptase activity associated with the reconstitution of the single-shelled rotavirus particle. Recombinant VP6 polypeptide was able to restore the transcriptional activity in purified viral cores from both SA-11 and RF rotavirus strains. Recombinant group C VP 6 (Cowden strain) is capable of binding as a trimer to group A viral core particles but unable to restore the transcriptase activity, suggesting that the binding of the polypeptide to cores is not the only requirement to restore the transcriptase activity. The VP 6 group A polypeptide was shown to bind as a monomer to viral cores, indicating that trimerization of VP 6 may be not required for reconstitution of the polymerase activity.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1993-09-01 | Archives of Virology |