Yeast surface display for screening combinatorial polypeptide libraries View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-06

AUTHORS

Eric T. Boder, K. Dane Wittrup

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-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. More... »

PAGES

553

Journal

TITLE

Nature Biotechnology

ISSUE

6

VOLUME

15

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nbt0697-553

    DOI

    http://dx.doi.org/10.1038/nbt0697-553

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1017819354

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9181578


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