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Yeast surface display for screening combinatorial polypeptide libraries.

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


  • Boder ET
  • Wittrup KD


Nature biotechnology

Publication Data

June 19, 1997

Associated Grants


Mesh Terms

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