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Abstract
AbstractWith the advancement of genetic engineering, monoclonal antibodies (mAbs) have made far-reaching progress in the treatment of various human diseases. However, due to the high cost of production, the increasing demands for antibody-based therapies have not been fully met. Currently, mAb-derived alternatives, such as antigen-binding fragments (Fab), single-chain variable fragments, bispecifics, nanobodies, and conjugated mAbs have emerged as promising new therapeutic modalities. They can be readily prepared in bacterial systems with well-established fermentation technology and ease of manipulation, leading to the reduction of overall cost. This review aims to shed light on the strategies to improve the expression, purification, and yield of Fab fragments in Escherichia coli expression systems, as well as current advances in the applications of Fab fragments.
Highlights
Since the first therapeutic monoclonal antibody drug was approved by the Food and Drug Administration (FDA), the past 30 years had witnessed substantial strides in the development of antibody therapeutics
Among the seven marketed Fab fragment drugs, only ranibizumab and certolizumab pegol are generated in E. coli as inclusion bodies (IBs), and the remaining Fabs are produced by cleavage of IgG with papain. ►Table 2 lists the monoclonal Fab antibody fragments approved by FDA
Among seven marketed Fab fragment drugs, only ranibizumab and certolizumab pegol are generated in E. coli as IBs
Summary
Since the first therapeutic monoclonal antibody (mAb) drug was approved by the Food and Drug Administration (FDA), the past 30 years had witnessed substantial strides in the development of antibody therapeutics. Molecular Chaperones Co-expression of molecular chaperons can decrease accumulation of IBs and can assist proteins in adopting the correct conformation These chaperons are foldases tailored to help trigger protein folding by interacting with the expressed proteins and form a protein–chaperon complex.[50] It is well documented that co-expression with molecular chaperons improves solubility and proper folding of various recombinant proteins and antibody fragments.[38] DnaK chaperones act in an ATP-dependent manner and cooperate with DnaJ and GrpE co-chaperones to mediate protein folding under both normal and stressful growth conditions.[51] Dsb (disulfide bond) enzymes A–G are found within the periplasm and are involved in the catalysis of disulfide bonds.[34] DsbA typically catalyzes disulfide bond formation in folding proteins while DsbC functions as a disulfide isomerase. Several other chromatographic techniques, including antigen affinity, ione[44] Strategies and Applications of Fab Production in Escherichia coli Chen et al
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