Research abstract
Brief Communications abstract
Nature Biotechnology 25, 563 - 565 (2007)
Published online: 15 April 2007 | doi:10.1038/nbt1296
Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli
Yariv Mazor1,3, Thomas Van Blarcom1,3, Robert Mabry1,2, Brent L Iverson1,2 & George Georgiou1,3,4,5
We describe facile isolation of full-length IgG antibodies from combinatorial libraries expressed in E. coli. Full-length heavy and light chains are secreted into the periplasm, where they assemble into aglycosylated IgGs that are captured by an Fc-binding protein that is tethered to the inner membrane. After permeabilizing the outer membrane, spheroplast clones expressing so-called E-clonal antibodies, which specifically recognize fluorescently labeled antigen, are selected using flow cytometry. Screening of a library constructed from an immunized animal yielded several antibodies with nanomolar affinities toward the protective antigen of Bacillus anthracis.
- Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.
- Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, Texas 78712, USA.
- Department of Chemical Engineering, University of Texas at Austin, Austin, Texas 78712, USA.
- Department of Biomedical Engineering, University of Texas at Austin, Austin, Texas 78712, USA.
- Section of Molecular Genetics and Microbiology, University of Texas at Austin, Austin, Texas 78712, USA.
Correspondence to: George Georgiou1,3,4,5 e-mail: gg@che.utexas.edu
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