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

Citation
Xg. Chen et al., High-level expression and purification of immunogenic recombinant SAG1 (P30) of Toxoplasma gondii in Escherichia coli, PROT EX PUR, 23(1), 2001, pp. 33-37
Citations number
9
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN EXPRESSION AND PURIFICATION
ISSN journal
1046-5928 → ACNP
Volume
23
Issue
1
Year of publication
2001
Pages
33 - 37
Database
ISI
SICI code
1046-5928(200110)23:1<33:HEAPOI>2.0.ZU;2-M
Abstract
Surface antigen 1 (SAG1) of Toxoplasma gondii is a good candidate for diagn osis and vaccine development, but recombinant SAG1 produced in Escheichia c oli often loses its specific immunogenicity due to the incorrect folding. I n 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 recogniz ed by human Toxoplasma-infective serum, and ELISA kits constructed by rSAG1 can sensitively and specifically detect toxoplasma infection. (C) 2001 Aca demic Press.