Surface Display of Recombinant Proteins onBacillus subtilisSpores

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Abstract
We developed a novel surface display system based on the use of bacterial spores. A protein of theBacillus subtilisspore coat, CotB, was found to be located on the spore surface and used as fusion partner to express the 459-amino-acid C-terminal fragment of the tetanus toxin (TTFC). Western, dot blot and fluorescent-activated cell sorting analyses were used to monitor TTFC surface expression on purified spores. We estimated that more than 1.5 × 103TTFC molecules were exposed on the surface of each spore and recognized by TTFC-specific antibodies. The efficient surface presentation of the heterologous protein, together with the simple purification procedure and the high stability and safety record ofB. subtilisspores, makes this spore-based display system a potentially powerful approach for surface expression of bioactive molecules.