Engineering protein glycosylation in prokaryotes. Issue 5 (October 2017)

• Record Type: Journal Article
• Authors: Keys, Timothy G.; Aebi, Markus
• Is Part Of: Current opinion in systems biology. Issue 5(2017)
• Page Start: 23
• Page End: 31
• Publication Date: 2017-10
• Subjects: Glycoengineering -- Glycoprotein -- N-glycosyltransferase -- Oligosaccharyltransferase -- PglB; Systems biology -- Periodicals; 570
• DOI: 10.1016/j.coisb.2017.05.016
• Languages: English
• ISSNs: 2452-3100

Abstract

Abstract: Controlling the specific glycan structure(s) present on a glycoprotein is a key challenge for both understanding its function and for developing effective next generation medical reagents. A decade ago the first engineered glycoproteins were produced in bacteria using the N-glycosylation machinery of Campylobacter jejuni . From the extensive development of this system, we learn the requisite features of a successful glycoengineering platform, as well as the factors that limit application in both glycan and protein structural space. From this perspective we review recent developments in the field of prokaryotic protein glycosylation. We highlight the emergence of cytoplasmic glycosylation systems as likely candidates to fuel the next wave of targeted glycoprotein synthesis with applications in research and medicine. Graphical abstract: Highlights: Only a small part of interesting glycoprotein structural space has been explored. Access to novel glycoproteins is limited by the available biosynthetic routes. Engineered periplasmic glycosylation can be used to make conjugate vaccines. Next generation glycoengineering will be based on novel cytoplasmic pathways.