Jorba N, Area E, Ortín J. Oligomerization of the influenza virus polymerase complex in vivo. J Gen Virol. 2008 Feb;89(Pt 2):520-4
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.
See Also:
- http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=18198383&dopt=AbstractPlus
Latest articles in those days:
- Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation 22 hours ago
- Risk assessment of a highly pathogenic H5N1 influenza virus from mink 23 hours ago
- Detection of clade 2.3.4.4b highly pathogenic H5N1 influenza virus in New York City 23 hours ago
- Sequence-based epitope mapping of high pathogenicity avian influenza H5 clade 2.3.4.4b in Latin America 2 days ago
- Guanylate-binding protein 1 inhibits inflammatory factors produced by H5N1 virus through Its GTPase activity 2 days ago
[Go Top] [Close Window]