4.4 Review

N-Linked glycoengineering for human therapeutic proteins in bacteria

期刊

BIOTECHNOLOGY LETTERS
卷 32, 期 9, 页码 1189-1198

出版社

SPRINGER
DOI: 10.1007/s10529-010-0289-6

关键词

N-Linked glycosylation; Therapeutic proteins; Campylobacter jejuni; E. coli; Metabolic engineering

资金

  1. UK's Biotechnology and Biological Sciences Research Council (BBSRC) [BBF0048421]
  2. Engineering and Physical Sciences Research Council (EPSRC) [EP/E036252/1]
  3. BBSRC [BB/F004842/1] Funding Source: UKRI
  4. EPSRC [EP/E036252/1] Funding Source: UKRI
  5. Biotechnology and Biological Sciences Research Council [BB/F004842/1] Funding Source: researchfish
  6. Engineering and Physical Sciences Research Council [EP/E036252/1] Funding Source: researchfish

向作者/读者索取更多资源

Approx. 70% of human therapeutic proteins are N-linked glycoproteins, and therefore host cells for production must contain the relevant protein modification machinery. The discovery and characterisation of the N-linked glycosylation pathway in the pathogenic bacterium Campylobacter jejuni, and subsequently its functional transfer to Escherichia coli, presents the opportunity of using prokaryotes as cell factories for therapeutic protein production. Not only could bacteria reduce costs and increase yields, but the improved feasibility to genetically control microorganisms means new and improved pharmacokinetics of therapeutics is an exciting possibility. This is a relatively new concept, and progress in bacterial N-glycosylation characterisation is reviewed and metabolic engineering targets revealed.

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