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Yeast surface display for screening combinatorial polypeptide libraries

Nature Biotechnology volume 15, pages 553–557 (1997)Cite this article

Abstract

Display on the yeast cell wall is well suited for engineering mammalian cell-surface and secreted proteins (e.g., antibodies, receptors, cytokines) that require endoplasmic reticulum-specif ic post-translational processing for efficient folding and activity. C-terminal fusion to the Aga2p mating adhesion receptor of Saccharomyces cerevisiae has been used for the selection of scFv antibody fragments with threefold decreased antigen dissociation rate from a randomly mutated library. A eukaryotic host should alleviate expression biases present in bacterially propagated combinatorial libraries. Quantitative flow cytometric analysis enables fine discrimination of kinetic parameters for protein binding to soluble ligands.

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Authors and Affiliations

  1. Department of Chemical Engineering, University of Illinois, Urbana, IL, 61801

    Eric T. Boder & K. Dane Wittrup

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  1. Eric T. Boder
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  2. K. Dane Wittrup
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Correspondence to K. Dane Wittrup.

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Boder, E., Wittrup, K. Yeast surface display for screening combinatorial polypeptide libraries. Nat Biotechnol 15, 553–557 (1997). https://doi.org/10.1038/nbt0697-553

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