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Título: | Oligomerization of the influenza virus polymerase complex in vivo |
Autor: | Jorba, Núria; Area, Estela; Ortín, Juan CSIC ORCID | Palabras clave: | Influenza A virus Polymerase complex Heterotrimer Tandem affinity purification (TAP) Higher-order oligomers |
Fecha de publicación: | feb-2008 | Editor: | Society for General Microbiology | Citación: | Journal of General Virology 89: 520-524 (2008) | Resumen: | The influenza virus polymerase is a heterotrimer formed by the PB1, PB2 and PA subunits and is responsible for virus transcription and replication. We have expressed the virus polymerase complex by co-transfection of the subunit cDNAs, one of which was tandem affinity purification (TAP)-tagged, into human cells. The intracellular polymerase complexes were purified by the TAP approach, involving two affinity chromatography steps, IgG–Sepharose and calmodulin–agarose. Gel-filtration analysis indicated that, although most of the purified polymerase behaved as a heterotrimer, a significant proportion of the purified material migrated as polymerase dimers, trimers and higher oligomers. Co-purification of polymerase complexes alternatively tagged in the same subunit confirmed that the polymerase complex might form oligomers intracellularly. The implications of this observation for virus infection are discussed. | Descripción: | 5 pages.-- PMID: 18198383 [PubMed]. | Versión del editor: | http://dx.doi.org/10.1099/vir.0.83387-0 | URI: | http://hdl.handle.net/10261/9465 | DOI: | 10.1099/vir.0.83387-0 | ISSN: | 0022-1317 |
Aparece en las colecciones: | (CNB) Artículos |
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