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Yeast surface display for screening combinatorial polypeptide libraries.

Nature biotechnology | Jun 19, 1997

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.

Pubmed ID: 9181578 RIS Download

Mesh terms: Animals | Cloning, Molecular | Endoplasmic Reticulum | Escherichia coli | Flow Cytometry | Gene Expression | Genomic Library | Immunoglobulin Fragments | Kinetics | Mammals | Mating Factor | Membrane Fusion | Mutagenesis | Peptide Biosynthesis | Peptide Library | Peptides | Plasmids | Polymerase Chain Reaction | RNA Processing, Post-Transcriptional | Recombinant Fusion Proteins | Saccharomyces cerevisiae