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Preparation, purification and biological function of fusion protein of ovalbumin and HSP70-like protein 1
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Abstract:
Objective： To prepare, purify the recombinant proteins of HSP70-like protein 1(HSP70L1) with a large fragment of chicken ovalbumin (OVA) , and to investigate the bio-function of the fusion protein, providing a basis for further study of the effect and the mechanism of HSP70L1 as an adjuvant. Methods: The vector containing HSP70L1 cDNA and large fragment of OVA was constructed. The expression of OVA-HSP70L1 fusion protein was induced and the products were purified from inclusion bodies by His-Trap metal chelation chromatography and DEAE ion-exchange chromatography. The bio-activity of the fusion protein was examined by detecting its ability to activate dendritic cells and to promote the secretion of cytokines. Results: The vector was successfully constructed and the molecular weight of the fused OVA-HSP70L1 protein (with a purity of over 95%) was 68 000. The fusion protein effectively promoted the maturation of dendritic cells and the production of cytokines such as interleukin-12 and tumor necrosis factor-α. Conclusion: HSP70L1 may be an effective adjuvant in the fusion protein and it may also promote antigen specific Th1 type i mmol/Luno-responses.
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