The Npro product of classical swine fever virus interacts with IkappaBalpha, the NF-kappaB inhibitor

Doceul, Virginie, Charleston, Bryan, Crooke, Helen, Reid, Elizabeth, Powell, Penny and Seago, Julian (2008) The Npro product of classical swine fever virus interacts with IkappaBalpha, the NF-kappaB inhibitor. Journal of General Virology, 89 (8). pp. 1881-1889. ISSN 1465-2099

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Abstract

Classical swine fever virus (CSFV) belongs to the genus Pestivirus and is the causative agent of classical swine fever, a haemorrhagic disease of pigs. The virus replicates in host cells without activating interferon (IFN) production and has been reported to be an antagonist of double-stranded RNA-induced apoptosis. The N-terminal protease (N(pro)) of CSFV is responsible for this evasion of the host innate immune response. In order to identify cellular proteins that interact with the N(pro) product of CSFV, a yeast two-hybrid screen of a human library was carried out, which identified IkappaBalpha, the inhibitor of NF-kappaB, a transcription factor involved in the control of apoptosis, the immune response and IFN production. The N(pro)-IkappaBalpha interaction was confirmed using yeast two-hybrid analysis and additional co-precipitation assays. It was also shown that N(pro) localizes to both the cytoplasmic and nuclear compartments in stably transfected cells and in CSFV-infected cells. Following stimulation by tumour necrosis factor alpha, PK-15 cell lines expressing N(pro) exhibited transient nuclear accumulation of pIkappaBalpha, but no effect of CSFV infection on IkappaBalpha localization or NF-kappaB p65 activation was observed.

Item Type: Article
Uncontrolled Keywords: nf-kappa b,animals,viral proteins,humans,two-hybrid system techniques,i-kappa b proteins,kidney,endopeptidases,cell line,classical swine fever virus
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
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Depositing User: EPrints Services
Date Deposited: 25 Nov 2010 11:09
Last Modified: 28 Oct 2019 11:32
URI: https://ueaeprints.uea.ac.uk/id/eprint/12518
DOI: 10.1099/vir.0.83643-0

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