title: N-Linked glycoengineering for human therapeutic proteins in bacteria.
abstract: 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.
authors.affiliation: ChELSI Institute, Biological and Environmental Systems Group, Department of Chemical and Process Engineering, University of Sheffield, Mappin Street, Sheffield S1 3JD, UK.
authors.forename: Jagroop
authors.initials: J
authors.lastname: Pandhal
authors.forename: Phillip C
authors.initials: PC
authors.lastname: Wright
mesh_terms: D001709:Biotechnology / Q000379:methods*; D016123:Campylobacter jejuni / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism*; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism / Q000627:therapeutic use*; D006031:Glycosylation; D006801:Humans; D053858:Metabolic Networks and Pathways / Q000235:genetics; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism* / Q000627:therapeutic use*
chemical_list: D006023:Glycoproteins; D011994:Recombinant Proteins