Journal
CURRENT OPINION IN BIOTECHNOLOGY
Volume 30, Issue -, Pages 205-210Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.copbio.2014.07.006
Keywords
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Funding
- UK's Biotechnology and Biological Sciences Research Council (BBSRC)
- Engineering and Physical Sciences Research Council (EPSRC) through the Bioprocess Research Industry Club (BRIC) programme [BB/K011200/1]
- BBSRC [BB/K011200/1, BB/F004842/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K011200/1, BB/F004842/1] Funding Source: researchfish
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Chinese Hamster Ovary cells are the most popular host expression system for the large-scale production of human therapeutic glycoproteins, but, the race to engineer Escherichia coli to perform glycosylation is gathering pace. The successful functional transfer of an N-glycosylation pathway from Campylobacter jejuni to Escherichia coli in 2002 can be considered as the crucial first engineering step. Here, we discuss the recent advancements in the field of N-glycosylation of recombinant therapeutic proteins in E. coli cells, from the manipulation of glycan composition, to the improvement in glycosylation efficiency, along with the challenges that remain before E. coli can be available as an industry host cell for economically viable glycoprotein production.
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