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- W2393533484 abstract "Hsp70 contains an N-terminal 44kDa ATPase portion(HSP701-358) and a C-terminal 28kDa portion (HSP70359-610) .which contains the 18kDa peptide binding domain(aa359 -540) .Constructing a chimeric vector of major antigenic seg- ment of E protein and binding domain in methylotrophic yeast Pichia pastoris was prepared to examine whether binding domain can enhance the immunogenicity of major antigenic segment of E protein. The vector was constructed by routine mole- cular technique. Fusion genes were linked with a restriction site BamHI. Vectors were transformed into yeast X-33 by electroporation. The recombinant transformants were selected by Zeocin. Expression of the fusion protein in yeast was induced by the addition of methanol and analysed by SDS-PAGE and western blot. The chimeric vector was constructed successfully. Relative molecular mass (Mr) of the fusion protein was sized about 68kDa. The protein was produced at a yield of 97 mg per litter of culture and has specific antigenicity. To examine cell and body immune response after BALB/c mice were immunized with E-BD fusion protein expressed in Pichia pastoris . Mice were immunized i.p. on day 0 and day 21 .We measured proliferation of lymphocytes by MTT and determined liters of antibody by ELISA. These data tell us the fusion protein is a more powerful antigen than major antigenic segment of JEV E protein alone. The effectiveness of binding domain in eliciting a humoral and cellular response to an attached antigenic peptide in the absense of adjuvant was illustrated and affirms the potential utility of bindingdomain in vaccine development." @default.
- W2393533484 created "2016-06-24" @default.
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- W2393533484 date "2005-01-01" @default.
- W2393533484 modified "2023-09-23" @default.
- W2393533484 title "Construction of Chimeric JEV E-Bindingdomain Plasmid in Methylotrophic Yeast Pichia pastoris" @default.
- W2393533484 hasPublicationYear "2005" @default.
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