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- W2163312764 abstract "The putative reovirus RNA polymerase, protein λ3, was characterized using antiserum prepared against a TrpE-λ3 fusion protein synthesized in Escherichia coli. Immunofluorescence microscopy showed that λ3 accumulated in perinuclear inclusion bodies in reovirus-infected cells. Analysis of λ3 accumulation in infected cells indicates that, once synthesized, λ3 is quite stable throughout the course of infection. Anti-λ3 serum did not immunoprecipitate virions, core particles or iodinated surface proteins of either virions or cores. These results indicate that λ3 is located in the inner part of the core. Experiments involving urea denaturation of purified reovirus cores indicate that λ3 cannot be selectively removed from the core without total denaturation of the core structure. When the dsRNA genome was eliminated from the core, λ3 remained associated with the other viral proteins in the core. Thus, λ3 appears to be a stable, structural component of the reovirus core, not bound to genomic dsRNA or free in soluble form inside the core. La protéine λ3 du réovirus, décrite comme une ARN-polymérase, a été caractérisée au moyen d'un immunsérum préparé contre une protéine de fusion TrpE-λ3 synthétisée par Escherichia coli. La microscopie en immunofluorescence montre que λ3 s'est accumulée dans les corps d'inclusion périnucléaires des cellules infectées par le réovirus. L'analyse de l'accumulation de λ3 dans les cellules infectées indique que, une fois synthétisée, λ3 est tout à fait stable au cours de l'infection. Le sérum anti-λ3 n'a immunoprécipité ni les virions, ni les particules du core, ni les protéines de surface, marquées par l'iode, aussi bien des virions que des cores. Ces résultats indiquent que la protéine λ3 est localisée dans la partie intérieure du core. Les expériences employant la dénaturation par l'urée des cores purifiés de réovirus indiquent que λ3 ne peut être retirée sélectivement du core sans dénaturation totale de la structure du core. Quand le génome ARN bicaténaire a été éliminé du core, λ3 est restée associée aux autres protéines virales dans le core. Ainsi, λ3 apparaît comme une partie stable de la structure du core du réovirus, qui n'est pas liée au génome ARN bicaténaire ni libre sous forme soluble à l'intérieur du core du virus." @default.
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- W2163312764 date "1994-01-01" @default.
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- W2163312764 title "Characterization and structural localization of the reovirus λ3 protein" @default.
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- W2163312764 doi "https://doi.org/10.1016/s0923-2516(07)80032-x" @default.
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