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1: Nat Biotechnol. 2007 May;25(5):563-5. Epub 2007 Apr 15.
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Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli.

Mazor Y, Van Blarcom T, Mabry R, Iverson BL, Georgiou G.

Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA.

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.

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PMID: 17435747 [PubMed - indexed for MEDLINE]