Glycoengineering bioconjugate vaccines, therapeutics, and diagnostics in E. coli

Journal Article · 27 May 2019 · Glycobiology

DOI: https://doi.org/10.1093/glycob/cwz031 · OSTI ID:1566258

Harding, Christian M. ^[1]; Feldman, Mario F. ^[2]

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1. VaxNewMo, St. Louis, MO, USA
2. VaxNewMo, St. Louis, MO, USA, Department of Molecular Microbiology, Washington University School of Medicine in St. Louis, St. Louis, Missouri, USA

Abstract 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.

• Sponsoring Organization: USDOE
• Grant/Contract Number: R41AI136633-01
• OSTI ID: 1566258
• Journal Information: Glycobiology, Journal Name: Glycobiology Vol. 29 Journal Issue: 7; ISSN 1460-2423
• Publisher: Oxford University PressCopyright Statement
• Country of Publication: Country unknown/Code not available
• Language: English