Notice of RetractionProkaryotic Expression and Identification on the ag85a-mpb63 Fusion Gene of Mycobacterium bovis

Notice of Retraction

After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.

We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.

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To increase the antigenicity of the unity antigen, the DNA fragments of ag85a and mpb63 were fused by splicing by overlapping extension(SOE) polymerase chain reaction(PCR), and the fusion gene ag85a-mpb63 was cloned into pMD18-T vector,then we got the recombinant plasmid pMD-85a-63. pMD-85a-63 and pET28a(+) were digested by BamH 1 and EcoK 1 double enzymes. The purified ag85a-mpb63 fusion gene was subcloned into the expression vector pET28a(+), and the prokaryotic expression vector pET-85a-63 was constructed. Plasmid containing pET-85a-63 was transformed into competence Escherichia coli BL21(DE3).The bacterium was induced by isopropyl-β-D-thiogalactopyranoside(IPTG) and its lysates were loaded directly onto sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE), approximately 49 ku exogenous protein was observed on the SDS-PAGE. The protein was analyzed by using Western-blotting. The results indicated that the protein was of antigenic reactivity of Mycobacterium bovis. These results could serve as a basis for further studies on the usefulness of the fusion gene and its expression productin the development of subunit vaccine, DNA vaccine and diagnostic reagents against bovine tuberculosis.