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Yeast surface display for screening combinatorial polypeptide libraries
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DOI：10.1038/nbt0697-553.png)
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Abstract
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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-specific 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.
Keywords:
antibody engineering
combinatorial library
surface display
affinity maturation
scFv
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41.7
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1.2W
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10.1W
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