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VP2, matured from the polyprotein encoded by the genome of infectious bursal disease virus (IBDV), is the primary host-protective immunogen of this virus. The matured VP2 protein (mVP2) and two of mVP2 N-terminal truncated mutants were cloned and expressed in E. coli in this study. To obtain pure recombinant proteins for the development of an efficient subunit vaccine against IBDV infection, they were fused with six additional histidine residues at its C-terminus as a His-purification-tag. Following purification employing immobilized metal-ion (Ni2+) affinity chromatography (IMAC), all the E. coli-derived three proteins have the morphology of icosahedral particles of approximately 25 nm in diameter. To reduce the cost of resins used for IMAC, self-prepared immobilized metal-ion affinity membranes (IMAMs), which were commercial regenerated cellulose membranes that modified with IDA and immobilized with nickel ions, were also applied to directly purify mVP2H and two mutant proteins. Results indicated that particles formed by mVP2H and its truncated mutants can also be efficiently purified, a purification fold of 104 was reached. The abundant quantities of pure rVP2H particles coupled with their uniform dimensions facilitates an understanding of higher order structure of the immunogenic particles and can therefore result in improved vaccines against the virus.
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