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Design of glycan epitope toolbox: a novel pathway for protein N-glycosylation in the E. coli cytosol

Total Cost €


EC-Contrib. €






Project "Glycoli" data sheet

The following table provides information about the project.


Organization address
address: Raemistrasse 101
postcode: 8092

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Switzerland [CH]
 Project website
 Total cost 187˙419 €
 EC max contribution 187˙419 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2015
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2016
 Duration (year-month-day) from 2016-11-01   to  2018-10-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

Metabolic engineering of E. coli has been highly successful in producing diverse free oligosaccharides for research and commercial applications. Currently, we are poised to address the next major challenge: the site-specific synthesis of oligosaccharides directly onto proteins in the E. coli cytosol. In this project we aim at the metabolic engineering of an N-glycosylation pathway in the E. coli cytosol using heterologous glycosyltransferases (GTs) to produce defined glycoprotein structures. Starting point is the newly discovered family of cytosolic N-glycosyltransferases (NGT), which transfer a single glucose residue onto proteins at asparagine (N) residues in the N-X-S/T sequon. Co-expression of an NGT with a galactosyltransferase has been shown to yield N-linked lactose in the E. coli cytosol. This N-linked lactose is an ideal starting point for the design of cytosolic N-glycosylation pathways to synthesize important glycans on proteins. Two goals are delineated. 1) Bacterial GTs will be screened, and potentially engineered, for their ability to extend the N-lactose with defined sugars, thereby generating a diverse repertoire of glycans directly synthesized on proteins. The focus will be on screening of fucosyltransferases and efficient production of fucosylated oligosaccharides, as these are central glycan epitopes in diverse physiological processes. 2) The newly developed glycosylation pathways will be applied to a range of protein substrates in order to explore and address possible limitations of the glycosylation system. The result will be a well-characterized glycoengineering toolbox enabling the bottom-up production of defined glycoprotein structures in E. coli.


year authors and title journal last update
List of publications.
2018 Hanne L.P. Tytgat Franklin L. Nobrega John van der Oost Willem M. de Vos
Bowel Biofilms: Tipping Points between a Healthy and Compromised Gut?
published pages: , ISSN: 0966-842X, DOI: 10.3929/ethz-b-000304638
Trends in Microbiology 2019-04-18
2018 Sonja Bäumel, Hanne L. P. Tytgat, Birgit Nemec, Ruth Schmidt, Loo Wee Chia, Hauke Smidt
Fifty Percent Human - how art brings us in touch with our microbial cohabitants
published pages: 571-574, ISSN: 1751-7915, DOI: 10.1111/1751-7915.13285
Microbial Biotechnology 11/4 2019-03-20

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