Expression of human VEGF165 in silkworm (Bombyx mori L.) by using a recombinant baculovirus and its bioactivity assay

Journal of Biotechnology
Xiaofeng WuWeizheng Cui

Abstract

Silkworm larva has a lot of advantages as a "biofactory" to produce recombinant protein. A recombinant baculovirus, carrying cDNA encoding the 165 amino-acid long isoform of human vascular endothelial growth factor (VEGF) was successfully constructed for the large-scale production of this protein using silkworms as an in vivo host. The fifth-instar silkworm larvae were inoculated with the recombinant virus. Time-course expression analysis indicated that the expression level was highest at around 80 h post-infection and the recombinant protein was found mainly in the haemolymph. Therefore, the hemolymph was collected from the infected larvae and the recombinant protein was purified by using Nickel affinity chromatography under native condition. The expression level was estimated to be as high as approximately 426 microg per larva. Furthermore, the recombinant protein was characterized and was found biologically active in inducing endothelial cell proliferation in vitro.

References

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Citations

Apr 16, 2010·Applied Biochemistry and Biotechnology·Soledad ChazarraJosé Neptuno Rodríguez-López
Jul 21, 2014·Enzyme and Microbial Technology·Nguyen-Duc ChungMoon-Sik Yang
Nov 18, 2005·Protein Expression and Purification·Geum Young LeeIn Seok Bang
Mar 15, 2013·Acta Biomaterialia·Frederic MurschelGregory De Crescenzo
Nov 28, 2009·Molecular Biology Reports·Abolfazl BarzegariMohammad Saeid Hejazi

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