Articles written in Journal of Biosciences
Volume 40 Issue 3 September 2015 pp 477-485 Articles
Porcine circovirus type 2 (PCV2) is the primary infectious agent of PCV-associated disease (PCVAD) in swine. ORF4 protein is a newly identified viral protein of PCV2 and is involved in virus-induced apoptosis. However, the molecular mechanisms of ORF4 protein regulation of apoptosis remain unclear, especially given there is no information regarding any cellular partners of the ORF4 protein. Here, we have utilized the yeast two-hybrid assay and identified four host proteins (FHC, SNRPN, COX8A and Lamin C) interacting with the ORF4 protein. Specially, FHC was chosen for further characterization due to its important role in apoptosis. GST pull-down, subcellular co-location and co-immunoprecipitation assays confirmed that the PCV2 ORF4 protein indeed interacted with the heavy-chain ferritin, which is an interesting clue that will allow us to determine the role of the ORF4 protein in apoptosis.
Volume 43 Issue 5 December 2018 pp 947-957 Article
Classical swine fever (CSF) is a contagious disease with a high mortality rate and is caused by classical swine fever virus(CSFV). CSFV non-structural protein 4B (NS4B) plays a crucial role in CSFV replication and pathogenicity. However,precisely how NS4B exerts these functions remains unknown, especially as there are no reports relating to potential cellularpartners of CSFV NS4B. Here, a yeast two-hybrid (Y2H) system was used to screen the cellular proteins interacting withNS4B from a porcine alveolar macrophage (PAM) cDNA library. The protein screen along with alignment using the NCBIdatabase revealed 14 cellular proteins that interact with NS4B: DDX39B, COX7C, FTH1, MAVS, NR2F6, RPLP1,PSMC4, FGL2, MKRN1, RPL15, RPS3, RAB22A, TP53BP2 and TBK1. These proteins mostly relate to oxidoreductaseactivity, signal transduction, localization, biological regulation, catalytic activity, transport and metabolism by GO categories.Tank-binding kinase 1 (TBK1) was chosen for further confirmation. The NS4B-TBK1 interaction was furtherconfirmed by subcellular co-location, co-immunoprecipitation and glutathione S-transferase pull-down assays. This studyoffers a theoretical foundation for further understanding of the diversity of NS4B functions in relation to viral infection andsubsequent pathogenesis.
Volume 44 | Issue 5
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