Monoclonal Antibodies Production in E. coli: Advances and Prospects

Monoclonal antibodies (mAbs), which are soluble glycoproteins of approximately 150 kDa consisting of heavy and light chains, are widely used in the treatment of cancers and autoimmune diseases. In recent years, the production methods of mAbs and their derivatives have become diverse, with Escherichia coli (E. coli) emerging as an important host for the production of antibody fragments.

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Production Methods of mAbs in E. coli

E. coli offers rapid growth, low costs, ease of operation, and flexibility in expression within the cytoplasm, periplasm, or culture medium. In E. coli, antibody production is mainly categorized into periplasmic, cytoplasmic, and semi-oxidized cytoplasmic production, as well as cell-free protein synthesis (CFPS) systems. Periplasmic production has achieved high yields of functional full-length immunoglobulin G (FL-IgG) through optimized expression and secretion balance. Cytoplasmic production faces challenges due to the reducing environment, but functional FL-IgG has been successfully expressed by engineering strains to create an oxidative environment. The CFPS system has achieved efficient antibody production by adjusting translation initiation regions and adding chaperone proteins.

Antibody Characterization and Quality Control

Quality control of antibodies includes biochemical, biophysical, and biological characterizations. Biochemical characterization analyzes antibody structure, sequence, and glycosylation, among others. Biophysical characterization evaluates homogeneity, solubility, and stability. Biological characterization validates antibody bioactivity, including ADCC and CDC, among others. Although deglycosylated antibodies produced in E. coli lack certain Fc effector functions, studies have shown that their stability is similar to that of glycosylated antibodies and they exhibit similar therapeutic efficacy under tested conditions.

To restore or enhance the immune effects of deglycosylated antibodies, Fc domains can be engineered. For example, mutants that bind to FcɣRI can be screened to enhance ADCC effector function. These engineered antibodies demonstrate significant biological effects and therapeutic potential both in vitro and in vivo.

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In summary, the production of deglycosylated antibodies in E. coli has made important progress in the field of antibody production, reducing costs and improving quality. Although they lack certain Fc effector functions, through engineering design, they exhibit enhanced effector functions and therapeutic potential. It is anticipated that more deglycosylated antibodies produced in E. coli will enter clinical studies in the future.

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