Industrial production of recombinant therapeutics in <Emphasis Type="Italic">Escherichia coli</Emphasis> and its recent advancements |
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Authors: | Chung-Jr Huang Henry Lin Xiaoming Yang |
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Institution: | (1) Cell Sciences & Technology, AMGEN Inc, Thousand Oaks, CA, USA |
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Abstract: | Nearly 30% of currently approved recombinant therapeutic proteins are produced in Escherichia coli. Due to its well-characterized genetics, rapid growth and high-yield production, E. coli has been a preferred choice and a workhorse for expression of non-glycosylated proteins in the biotech industry. There is
a wealth of knowledge and comprehensive tools for E. coli systems, such as expression vectors, production strains, protein folding and fermentation technologies, that are well tailored
for industrial applications. Advancement of the systems continues to meet the current industry needs, which are best illustrated
by the recent drug approval of E. coli produced antibody fragments and Fc-fusion proteins by the FDA. Even more, recent progress in expression of complex proteins
such as full-length aglycosylated antibodies, novel strain engineering, bacterial N-glycosylation and cell-free systems further
suggests that complex proteins and humanized glycoproteins may be produced in E. coli in large quantities. This review summarizes the current technology used for commercial production of recombinant therapeutics
in E. coli and recent advances that can potentially expand the use of this system toward more sophisticated protein therapeutics. |
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