"Inclonals": IgGs and IgG-enzyme fusion proteins produced in an E. coli expression-refolding system

Rahely Hakim, Itai Benhar*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Full-length antibodies and antibodies that ferry a cargo to target cells are desired biopharmaceuticals. We describe the production of full-length IgGs and IgG-toxin fusion proteins in E. coli. In the presented examples of anti CD30 and anti EGF-receptor antibodies, the antibody heavy and light chains or toxin fusions thereof were expressed in separate bacterial cultures, where they accumulated as insoluble inclusion bodies. Following refolding and purification, high yields (up to 50 mg/L of shake flask culture) of highly purified (>90%) full-length antibodies and antibody-toxin fusions were obtained. The bacterially produced antibodies, named "Inclonals," equaled the performance of the same IgGs that were produced using conventional mammalian cell culture in binding properties as well as in cell killing potency. The rapid and cost effective IgG production process and the high quality of the resultant product may make the bacterial production of full-length IgG and IgG-drug fusion proteins an attractive option for antibody production and a significant contribution to recombinant antibody technology.

Original languageEnglish
Pages (from-to)281-287
Number of pages7
JournalmAbs
Volume1
Issue number3
DOIs
StatePublished - May 2009

Funding

FundersFunder number
Israel Cancer Research Fund

    Keywords

    • CD30
    • EGFR
    • IgG
    • IgG-toxin fusion protein
    • Inclusion bodies
    • PE38
    • Refolding

    Fingerprint

    Dive into the research topics of '"Inclonals": IgGs and IgG-enzyme fusion proteins produced in an E. coli expression-refolding system'. Together they form a unique fingerprint.

    Cite this