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J Gen Virol 89 (2008), 520-524; DOI 10.1099/vir.0.83387-0

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Short Communication

Oligomerization of the influenza virus polymerase complex in vivo

Núria Jorba, Estela Area{dagger} and Juan Ortín

Centro Nacional de Biotecnología (CSIC), Darwin 3, Campus de Cantoblanco, 28049 Madrid, Spain

Correspondence
Juan Ortín
jortin{at}cnb.uam.es

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.

{dagger}Present address: Department of Neurology, Columbia University, New York, NY 10033, USA.

A figure showing the control of the potential proteolysis of the influenza polymerase is available with the online version of this paper.




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