![]() The expression and display of proteins on the surface of bacterial and eukaryotic host cells has become increasingly attractive, as demonstrated by the numerous platform technologies that have been developed. The versatility of this screening platform will be emphasized by describing many examples of the engineering of non-antibody molecules as well as functional screening strategies for the modification of enzymes. This review focuses on directed evolution of alternative scaffolds and enzymes engineered to improved target binding, specificity or activity using yeast surface display. Ultra-high throughput yeast library screening has been extensively used in pharma and biotech industry for the screening of large antibody repertoires aimed at isolating variants with therapeutic relevance. Notably, the yeast Saccharomyces cerevisiae proved to be an invaluable tool for the generation of large protein libraries, where each variant is displayed in high copy number on the surface of a single cell, thereby converting gene diversity into cell diversity. The method was enabled by the emergence of cell surface display techniques that bring proteins of interest into direct contact with potential interaction partners. Directed evolution is a powerful method that involves (1) the random generation of a broad set of protein variants, (2) their production in an expression host, and (3) the subsequent screening for variants with desired novel functionalities.
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