Citation
Abstract
The hypervariable region (HVR) of VP2 protein of infectious bursal disease virus (IBDV) elicits neutralising antibodies, but it is highly hydrophobic and tends to form inclusion bodies when expressed in Escherichia coli. To improve its solubility, the VP2(HVR) was fused to the C-terminal end of Newcastle disease virus (NDV) nucleocapsid (NP) protein and expressed in E. coli TOP 10 cells under the control of trc promoter. However, the fusion protein, NP-VP2(HVR)-trc, aggregated into insoluble inclusion bodies in the host cells. Therefore the coding region of NP-VP2(HVR) was sub-cloned into expression vectors containing the T7 promoter. The solubility of the NP-VP2(HVR)-T7 fusion proteins improved dramatically in E. coli BL21 (DE3), BL21 (SI) and Origami B cells.
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Additional Metadata
Item Type: | Article |
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Divisions: | Faculty of Biotechnology and Biomolecular Sciences |
Publisher: | Universiti Putra Malaysia Press |
Keywords: | Newcastle disease virus; Infectious bursal disease virus; VP2 solubility; Hypervariable region. |
Depositing User: | Ms. Nida Hidayati Ghazali |
Date Deposited: | 02 Jul 2013 02:20 |
Last Modified: | 18 Sep 2015 03:01 |
URI: | http://psasir.upm.edu.my/id/eprint/17251 |
Statistic Details: | View Download Statistic |
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