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. 2001 Oct;23(1):33-7.
doi: 10.1006/prep.2001.1483.

High-level expression and purification of immunogenic recombinant SAG1 (P30) of Toxoplasma gondii in Escherichia coli

X G Chen  1 , Y Gong, Hua-Li, Z R Lun, M C Fung
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High-level expression and purification of immunogenic recombinant SAG1 (P30) of Toxoplasma gondii in Escherichia coli

X G Chen et al. Protein Expr Purif. 2001 Oct.

Abstract

Surface antigen 1 (SAG1) of Toxoplasma gondii is a good candidate for diagnosis and vaccine development, but recombinant SAG1 produced in Escheichia coli often loses its specific immunogenicity due to the incorrect folding. In the present study, a truncated SAG1 was highly expressed in E. coli as a fusion protein, about 30% of the total protein of the cell lysate. After a simple purification and refolding procedure, purified rSAG1 can be recognized by human Toxoplasma-infective serum, and ELISA kits constructed by rSAG1 can sensitively and specifically detect toxoplasma infection.

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