Making antibody fragments using phage display libraries View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-08

AUTHORS

T Clackson, H R Hoogenboom, A D Griffiths, G Winter

ABSTRACT

To by-pass hybridoma technology and animal immunization, we are trying to build antibodies in bacteria by mimicking features of immune selection. Recently we used fd phage to display antibody fragments fused to a minor coat protein, allowing enrichment of phage with antigen. Using a random combinatorial library of the rearranged heavy (VH) and kappa (V kappa) light chains from mice immune to the hapten 2-phenyloxazol-5-one (phOx), we have now displayed diverse libraries of antibody fragments on the surface of fd phage. After a single pass over a hapten affinity column, fd phage with a range of phOx binding activities were detected, at least one with high affinity (dissociation constant, Kd = 10(-8) M). A second pass enriched for the strong binders at the expense of the weak. The binders were encoded by V genes similar to those found in anti-phOx hybridomas but in promiscuous combinations (where the same V gene is found with several different partners). By combining a promiscuous VH or V kappa gene with diverse repertoires of partners to create hierarchical libraries, we elicited many more pairings with strong binding activities. Phage display offers new ways of making antibodies from V-gene libraries, altering V-domain pairings and selecting for antibodies with good affinities. More... »

PAGES

624-628

Journal

TITLE

Nature

ISSUE

6336

VOLUME

352

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/352624a0

    DOI

    http://dx.doi.org/10.1038/352624a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1021945431

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1907718


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