| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2020599 | Protein Expression and Purification | 2012 | 7 Pages |
Interferon beta (IFN-β) belongs to a class of natural proteins that can inhibit virus replication. In this paper, nucleic acid sequence encoding chicken interferon beta (chIFN-β) mature protein was cloned and highly expressed in Escherichia coli (E. coli) by 1 mM IPTG induction. The expressed chIFN-β was about 20% of total bacterial protein. The recombinant protein in form of inclusion body was then solubilised, refolded and purified to a purity of greater than 95% by immobilized metal ion affinity chromatography (IMAC). This recombinant chIFN-β could inhibit vesicular stomatitis Indiana virus (VSV) and infectious bursal disease virus (IBDV) replication in vitro. Animal experiments showed that the recombinant chIFN-β could decrease pathological lesions caused by the IBDV in bursa of Fabricius. These results will provide useful information for further investigations on veterinary clinical applications and fundamental research.
► All the mistakes and shortcomings have been corrected or been further explained. ► The sequenced map of chIFN-β mature protein gene has been uploaded. ► The pathological lesions of bursa of Fabricius have been re-analysed. ► Some pictures have been optimised and the description have been re-written.
