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Título

Oligomerization of the influenza virus polymerase complex in vivo

Autor Jorba, Núria; Area, Estela; Ortín, Juan
Palabras clave Influenza A virus
Polymerase complex
Heterotrimer
Tandem affinity purification (TAP)
Higher-order oligomers
Fecha de publicación feb-2008
EditorSociety for General Microbiology
Citación Journal of General Virology 89: 520-524 (2008)
ResumenThe 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 editorhttp://dx.doi.org/10.1099/vir.0.83387-0
URI http://hdl.handle.net/10261/9465
DOI10.1099/vir.0.83387-0
ISSN0022-1317
Aparece en las colecciones: (CNB) Artículos
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