Molecular display, a technique that presents proteins or peptides on the surface of microorganisms, enables high-throughput screening and has become an essential tool in bimolecular engineering. To display properly, the proteins should be fused to a display motif, translocated through the membrane, and anchored at the cell surface. Many surface proteins, for example, Lpp-ompA, InaK and AIDA-I from Escherichia coli, have been used for displaying target proteins, such as antigens, enzymes, and bioadsorbents [1]. Here, we discuss the unique molecular display system of Bacillus spores: (i) the spore is the most resilient life form; (ii) no secretion is required for the display; and (iii) the foreign proteins can be displayed in their native forms, thus obviating the need to produce fusion proteins.
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