TY - JOUR
T1 - Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli
AU - Harding, Christian M.
AU - Feldman, Mario F.
N1 - Funding Information:
This work was supported by a National Institute of Allergy and Infectious Disease Small Business Technology Transfer grant (R41AI136633-01).
Publisher Copyright:
© 2019 The Author(s) 2019. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: [email protected].
PY - 2019/7/1
Y1 - 2019/7/1
N2 - The first, general glycosylation pathway in bacteria, the N-linked glycosylation system of Campylobacter jejuni, was discovered two decades ago. Since then, many diverse prokaryotic glycosylation systems have been characterized, including O-linked glycosylation systems that have no homologous counterparts in eukaryotic organisms. Shortly after these discoveries, glycosylation pathways were recombinantly introduced into E. coli creating the field of bacterial glycoengineering. Bacterial glycoengineering is an emerging biotechnological tool that harnesses prokaryotic glycosylation systems for the generation of recombinantly glycosylated proteins using E. coli as a host. Over the last decade, as our understanding of prokaryotic glycosylation systems has advanced, so too has the glycoengineering toolbox. Currently, glycoengineering utilizes two broad approaches to recombinantly glycosylate proteins, both of which can generate N-or O-linkages: oligosaccharyltransferase (OTase)-dependent and OTase-independent. This review discusses the applications of these bacterial glycoengineering techniques as they relate to the development of glycoconjugate vaccines, therapeutic proteins, and diagnostics.
AB - The first, general glycosylation pathway in bacteria, the N-linked glycosylation system of Campylobacter jejuni, was discovered two decades ago. Since then, many diverse prokaryotic glycosylation systems have been characterized, including O-linked glycosylation systems that have no homologous counterparts in eukaryotic organisms. Shortly after these discoveries, glycosylation pathways were recombinantly introduced into E. coli creating the field of bacterial glycoengineering. Bacterial glycoengineering is an emerging biotechnological tool that harnesses prokaryotic glycosylation systems for the generation of recombinantly glycosylated proteins using E. coli as a host. Over the last decade, as our understanding of prokaryotic glycosylation systems has advanced, so too has the glycoengineering toolbox. Currently, glycoengineering utilizes two broad approaches to recombinantly glycosylate proteins, both of which can generate N-or O-linkages: oligosaccharyltransferase (OTase)-dependent and OTase-independent. This review discusses the applications of these bacterial glycoengineering techniques as they relate to the development of glycoconjugate vaccines, therapeutic proteins, and diagnostics.
KW - E. coli
KW - bioconjugate
KW - glycoengineering
KW - glycosyltransferase
KW - oligosaccharyltransferase
UR - http://www.scopus.com/inward/record.url?scp=85068488597&partnerID=8YFLogxK
U2 - 10.1093/glycob/cwz031
DO - 10.1093/glycob/cwz031
M3 - Review article
C2 - 30989179
AN - SCOPUS:85068488597
SN - 0959-6658
VL - 29
SP - 519
EP - 529
JO - Glycobiology
JF - Glycobiology
IS - 7
M1 - cwz031
ER -