Abstract
Objective To investigate the chaperone activity of Chlamydia trachomatis (Ct)recombinant fusion protein DsbG on elementary body (EB)infectivity to HeLa229 cell.Methods Ct recombinant fusion protein DsbG was cloned,expressed and purified with regular procedure.HeLa229 cell was cultured with 24 ×cells plate in density mono-layer.Three means including labeling EB with isotope 35S,renaturation of 8 mol/L urea-denatured citrate synthase (CS)and counting inclusion body after indirect immunofluorescence mediated by Ct major outer membrane protein (MOMP)mono-antibody were employed to study chaperone activity of recombinant fusion protein DsbG.Results After incubating Ct EB with recombinant fusion protein DsbG for 30 min,absorption rate of EB to host cell was raised and exist significant difference when compared with placebo (P＜0.05),the renaturation time for 8 mol/L urea-denatured CS was shorten,furthermore,DsbG can protect EB from damage when incubated in 37%for 60 min and sustained the infectivity to host cell,so as to increase inclusion body by 32%when compared with placebo.Conclusion As a disulfide bond isomerase,DsbG may also have chaperone activity during EB infecting to host cell. Key words: Chlamydia trachomatis; Disulfide bond; DsbG; Chaperone
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