Enhanced production of full-length immunoglobulin G via the signal recognition particle (SRP)-dependent pathway in Escherichia coli

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Because of the lack of post-translational glycosylation, Escherichia coil is not a preferable host for immunoglobulin G (IgG) production. However, recent successes in the developments of aglycosylated IgG variants that do not require glycosylation for effector functions have increased the likelihood of using E. coil for IgG production. Here, we have developed a new E. coil host-vector system for enhanced production of recombinant IgG using: (i) a combination of SRP/Sec-dependent pathways for the efficient secretion of heavy and light chains in the periplasm; (ii) co-expression of periplasmic foldase (DsbC) for efficient assembly of IgG in the periplasm; and (iii) co-expression of Ffh for enhancing the SRP machinery. Finally, with engineered host-vector system, fed-batch cultivations were conducted at four different conditions, and under an optimized condition, up to 62 mg/L of active full-length IgG was produced during a 28-h cultivation. (C) 2013 Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2013-05
Language
English
Article Type
Article
Keywords

DISULFIDE BOND FORMATION; HIGH-LEVEL EXPRESSION; ANTIBODIES; PROTEIN; GLYCOSYLATION; TRANSLOCATION; STRATEGIES; MEMBRANE; CULTURE

Citation

JOURNAL OF BIOTECHNOLOGY, v.165, no.2, pp.102 - 108

ISSN
0168-1656
DOI
10.1016/j.jbiotec.2013.03.007
URI
http://hdl.handle.net/10203/174036
Appears in Collection
CBE-Journal Papers(저널논문)
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