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The expression of recombinant proteins on the external surface of Gram-negative bacteria is expected to open the way for a number of significant biotechnological applications, including the development of live bacterial vaccines, the production of whole cell adsorbents, the preparation of whole cell catalysts, and the display and selection of peptide and antibody libraries. We have developed a fusion protein system for the production of active recombinant proteins on the surface of Escherichia coli. Using this system we have expressed beta-lactamase, the Cellulomonas fimi exoglucanase Cex as well as its cellulose binding domain, and an antidigoxin single chain Fv antibody fragment on the cell surface. Recently we have begun to explore some of the potential applications for cell-surface expression.
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Francisco et al. (1994) studied this question.
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