Abstract
Objective To express and purify rESAT-6-CFP-10( rEC) fusion protein of Mycobacterium tuberculosis H37Rv and evaluate its application in tuberculosis serodiagnosis. Methods The rEC fusion protein was purified by nickel-chelate affinity chromatography, and anti-tuberculosis antibody was analyzed by ELISA, the specificity and sensitivity of rEC were evaluated by the positive cut off value determined as A492 + 2s in 37 serum samples from PPD-negative healthy people. Results The rEC fusion protein existed in soluble form in E. coli, and the concentration was 0.19 mg/mL. The specificity in PPD-positive healthy people was 100%(30/30) by anti-tuberculosis antibody detection of rEC, and the sensitivity in smear or germiculture positive and negative tuberculosis patients were 75.56%(34/45) and 67.31%(35/52), respectively. Conclusions The rEC fusion protein can be highly expressed in soluble form in E. coli. It has good immunoreactivity and serodiagnosis value. Key words: Mycobacterium tuberculosis; rESAT-6-CFP-10 fusion protein; Serodiagnosis
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