Evidence map›Paper›PMID 34405535›Full record

ArticleMicrobial biotechnology2021

DisCoTune: versatile auxiliary plasmids for the production of disulphide-containing proteins and peptides in the E. coli T7 system.

Andreas B Bertelsen, Celeste Menuet Hackney, Carolyn N Bayer, Lau D Kjelgaard, Maja Rennig, Brian Christensen, Esben Skipper Sørensen, Helena Safavi-Hemami, Tune Wulff, Lars Ellgaard and 1 more

Abstract read
In one paragraph

Article in Microbial biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Production of Antibody Fragments Suitable for 1:1, Site-Specific Labeling.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. Structural similarities reveal an expansive conotoxin family with a two-finger toxin fold.Protein science : a publication of the Protein Society · 2025
    Article
  7. Article
  8. Review
  9. Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
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

11 authors.

Andreas B BertelsenThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Celeste Menuet HackneyDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen N., 2200, Denmark.
Carolyn N BayerThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Lau D KjelgaardDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen N., 2200, Denmark.ORCID 0000-0001-5352-0809
Maja RennigThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Brian ChristensenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, 8000, Denmark.
Esben Skipper SørensenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus C, 8000, Denmark.ORCID 0000-0002-7050-3354
Helena Safavi-HemamiDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen N., 2200, Denmark.ORCID 0000-0002-1984-2721
Tune WulffThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.
Lars EllgaardDepartment of Biology, Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen N., 2200, Denmark.ORCID 0000-0002-7018-0137
Morten H H NørholmThe Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, 2800, Denmark.ORCID 0000-0002-7871-5191

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Secreted proteins and peptides hold large potential both as therapeutics and as enzyme catalysts in biotechnology. The high stability of many secreted proteins helps maintain functional integrity in changing chemical environments and is a contributing factor to their commercial potential. Disulphide bonds constitute an important post-translational modification that stabilizes many of these proteins and thus preserves the active state under chemically stressful conditions. Despite their importance, the discovery and applications within this group of proteins and peptides are limited by the availability of synthetic biology tools and heterologous production systems that allow for efficient formation of disulphide bonds. Here, we refine the design of two DisCoTune (Disulphide bond formation in E. coli with tunable expression) plasmids that enable the formation of disulphides in the highly popular Escherichia coli T7 protein production system. We show that this new system promotes significantly higher yield and activity of an industrial protease and a conotoxin, which belongs to a group of disulphide-rich venom peptides from cone snails with strong potential as research tools and pharmacological agents.

Indexed as

DisulfidesEscherichia coliPeptidesPlasmidsProtein FoldingDisulfidesPeptides

Identifiers

PMID34405535
PMCPMC8601162

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Registered trials

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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.