title: Bacterial expression systems for recombinant protein production: E. coli and beyond.
abstract: Escherichia coli expression system continues to dominate the bacterial expression systems and remain to be the preferred system for laboratory investigations and initial development in commercial activities or as a useful benchmark for comparison among various expression platforms. Some new developments in overcoming its shortcomings are reviewed in this paper, including antibiotics-free selection plasmids, extracellular production, and posttranslational modifications. The ability for E. coli to make mg glycosylated proteins promises even broader applications of the E. coli system in the future. Significant progresses have also been made over the past few years in alternative bacterial expression systems. Notably, the Lactoccocus lactis system has proven to be a viable choice for membrane proteins. Additionally, several Pseudomonas systems were developed and achieved product titers comparable to E. coli systems. Other bacterial systems such as Streptomyces, coryneform bacteria, and halophilic bacteria offer advantages in some niche areas, providing more choices of bacterial expression systems for recalcitrant proteins.
authors.affiliation: School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0100, United States. rchen@chbe.gatech.edu
authors.forename: Rachel
authors.initials: R
authors.lastname: Chen
mesh_terms: D004926:Escherichia coli / Q000378:metabolism*; D008565:Membrane Proteins / Q000096:biosynthesis; D010957:Plasmids / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011549:Pseudomonas / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis*
chemical_list: D008565:Membrane Proteins; D011994:Recombinant Proteins