Evidence map›Paper›PMID 29863724›Full record

ArticleNature biotechnology2018

Custom selenoprotein production enabled by laboratory evolution of recoded bacterial strains.

Ross Thyer, Raghav Shroff, Dustin R Klein, Simon d'Oelsnitz, Victoria C Cotham, Michelle Byrom, Jennifer S Brodbelt, Andrew D Ellington

Abstract read
In one paragraph

Article in Nature biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023
    Article
  10. Recent progress in adaptive laboratory evolution of industrial microorganisms.Journal of industrial microbiology & biotechnology · 2023
    Article
  11. Creating Selenocysteine-Specific Reporters Using Inteins.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

8 authors at 1 institution in 1 country.

Ross ThyerCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA.
Raghav ShroffCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA.
Dustin R KleinDepartment of Chemistry, University of Texas at Austin, Austin, Texas, USA.
Simon d'OelsnitzCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA.
Victoria C CothamDepartment of Chemistry, University of Texas at Austin, Austin, Texas, USA.
Michelle ByromCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA.
Jennifer S BrodbeltDepartment of Chemistry, University of Texas at Austin, Austin, Texas, USA.
Andrew D EllingtonCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA.
The University of Texas at Austin · US

Funding

Recombinant antibodies containing L-DOPA for stability, functionalization and selectionK99CA207870 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI THYER, ROSS T · 2016 to 2017
$186k
NCI NIH HHS K99 CA207870
6 · The paper itself

Abstract

Incorporation of the rare amino acid selenocysteine to form diselenide bonds can improve stability and function of synthetic peptide therapeutics. However, application of this approach to recombinant proteins has been hampered by heterogeneous incorporation, low selenoprotein yields, and poor fitness of bacterial producer strains. We report the evolution of recoded Escherichia coli strains with improved fitness that are superior hosts for recombinant selenoprotein production. We apply an engineered β-lactamase containing an essential diselenide bond to enforce selenocysteine dependence during continuous evolution of recoded E. coli strains. Evolved strains maintain an expanded genetic code indefinitely. We engineer a fluorescent reporter to quantify selenocysteine incorporation in vivo and show complete decoding of UAG codons as selenocysteine. Replacement of native, labile disulfide bonds in antibody fragments with diselenide bonds vastly improves resistance to reducing conditions. Highly seleno-competent bacterial strains enable industrial-scale selenoprotein expression and unique diselenide architecture, advancing our ability to customize the selenoproteome.

Indexed as

Directed Molecular Evolutionbeta-LactamasesDisulfidesEscherichia coliGene Expression Regulation, BacterialSelenocysteineSelenoproteinsbeta-LactamasesDisulfidesSelenocysteineSelenoproteins

Identifiers

PMID29863724
PMCPMC6035053
OpenAlexW2806189034

What OpenQuestion holds

Textmetadata
LicenceTDM
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.