Evidence map›Paper›PMID 31776333›Full record

ArticleNature communications2019

Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies.

Hanne L P Tytgat, Chia-Wei Lin, Mikail D Levasseur, Markus B Tomek, Christoph Rutschmann, Jacqueline Mock, Nora Liebscher, Naohiro Terasaka, Yusuke Azuma, Michael Wetter and 4 more

Abstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed.

  1. Article
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  5. Construction of anFrontiers in bioengineering and biotechnology · 2024
    Article
  6. Review
  7. Article
  8. Review
  9. Article
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  11. Post-Assembly Modification of Protein Cages by Ubc9-Mediated Lysine Acylation.Chembiochem : a European journal of chemical biology · 2022
    Article
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
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  18. Article
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  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors.

Hanne L P TytgatInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-6270-2110
Chia-Wei LinInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4777-2916
Mikail D LevasseurLaboratory of Organic Chemistry, ETH Zurich, 8093, Zurich, Switzerland.
Markus B TomekInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-0492-975X
Christoph RutschmannInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.
Jacqueline MockInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4618-1113
Nora LiebscherInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.
Naohiro TerasakaLaboratory of Organic Chemistry, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4988-6899
Yusuke AzumaLaboratory of Organic Chemistry, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-3543-3159
Michael WetterInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-6998-7697
Martin F BachmannDepartment of Immunology, Inselspital, University of Bern, 3010, Bern, Switzerland.
Donald HilvertLaboratory of Organic Chemistry, ETH Zurich, 8093, Zurich, Switzerland.
Markus AebiInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland.
Timothy G KeysInstitute of Microbiology, ETH Zurich, 8093, Zurich, Switzerland. tim.keys@micro.biol.ethz.ch.ORCID http://orcid.org/0000-0003-2921-0362

Funding

Austrian Science Fund FWF J 4230
6 · The paper itself

Abstract

Glycosylation of proteins profoundly impacts their physical and biological properties. Yet our ability to engineer novel glycoprotein structures remains limited. Established bacterial glycoengineering platforms require secretion of the acceptor protein to the periplasmic space and preassembly of the oligosaccharide substrate as a lipid-linked precursor, limiting access to protein and glycan substrates respectively. Here, we circumvent these bottlenecks by developing a facile glycoengineering platform that operates in the bacterial cytoplasm. The Glycoli platform leverages a recently discovered site-specific polypeptide glycosyltransferase together with variable glycosyltransferase modules to synthesize defined glycans, of bacterial or mammalian origin, directly onto recombinant proteins in the E. coli cytoplasm. We exploit the cytoplasmic localization of this glycoengineering platform to generate a variety of multivalent glycostructures, including self-assembling nanomaterials bearing hundreds of copies of the glycan epitope. This work establishes cytoplasmic glycoengineering as a powerful platform for producing glycoprotein structures with diverse future biomedical applications.

Indexed as

BenzazepinesCytoplasmEpitopesEscherichia coliGlucoseGlucosyltransferasesGlycoproteinsGlycosylationGreen Fluorescent ProteinsMetabolic EngineeringMonosaccharidesPolysaccharidesPromoter Regions, GeneticRecombinant ProteinsBenzazepinesEpitopesGlucoseGlucosyltransferasesGlycoproteinsGreen Fluorescent ProteinsMonosaccharidesN-glucosylvareniclinePolysaccharidesRecombinant Proteins

Identifiers

PMID31776333
PMCPMC6881330

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.