Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-05

AUTHORS

Yariv Mazor, Thomas Van Blarcom, Robert Mabry, Brent L Iverson, George Georgiou

ABSTRACT

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. More... »

PAGES

563-565

References to SciGraph publications

Journal

TITLE

Nature Biotechnology

ISSUE

5

VOLUME

25

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1296

DOI

http://dx.doi.org/10.1038/nbt1296

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015036233

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17435747


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