Salmonella flagellin acted as an effective fusion partner for expression of Plasmodium falciparum surface protein 25 in Escherichia coli

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Abstract

Plasmodium falciparum surface protein 25 (Pfs25) is a hard-to-express and hard-to-solubilize protein in Escherichia coli. To overcome this problem, the phase 1 flagellin of Salmonella enterica serovar Typhimurium (FliC) was used as a fusion partner for Pfs25. The fusion expression of Pfs25 with FliC greatly enhanced the expression level and solubility of Pfs25 in E. coli BL21(DE3). The Ni-purified fusion protein of FliC-Pfs25 was recognized by two anti-Pfs25 monoclonal antibodies. By comparison, it was shown that the Pfs25 within FliC-Pfs25 contained epitopes similar or identical to those on Pichia pastoris-produced Pfs25. The data obtained from this study demonstrated that the fusion with Salmonella flagellin greatly improved the expression of Pfs25 in E. coli.

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Qian, F., Li, M., Chen, Y., Jiang, L., & Xu, H. (2016, September 1). Salmonella flagellin acted as an effective fusion partner for expression of Plasmodium falciparum surface protein 25 in Escherichia coli. Human Vaccines and Immunotherapeutics. Taylor and Francis Inc. https://doi.org/10.1080/21645515.2016.1171443

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