Evidence map›Paper›PMID 20601499›Full record

ArticleApplied and environmental microbiology2010

Display of recombinant proteins on Bacillus subtilis spores, using a coat-associated enzyme as the carrier.

Sébastien Potot, Cláudia R Serra, Adriano O Henriques, Ghislain Schyns

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  8. Article
  9. Advances in engineeredSynthetic and systems biotechnology · 2021
    Review
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  13. Review
  14. Article
  15. Article
  16. Article
  17. Biological Containment of Genetically Modified Bacillus subtilis.Applied and environmental microbiology · 2018
    Article
  18. Article
  19. Article
  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

4 authors at 1 institution in 1 country.

Sébastien PototDSM Nutritional Products, Ltd., Biotechnology R&D, 203/25a, P.O. Box 2676, CH-4002 Basel, Switzerland. .
Cláudia R Serra
Adriano O Henriques
Ghislain Schyns
Universidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The display of proteins such as feed enzymes at the surface of bacterial spore systems has a great potential use for animal feed. Feed enzymes increase the digestibility of nutrients, leading to greater efficiency in the manufacturing of animal products and minimizing the environmental impact of increased animal production. To deliver their full potential in the gut, feed enzymes must survive the harsh conditions of the feed preparation and the gastrointestinal tract. The well-documented resistance of spores to harsh environments, together with the ability to use proteins that compose the spore as carriers for the display of passenger proteins, suggests that spores could be used as innovative tools to improve the formulation of bioactive molecules. Although some successful examples have been reported, in which abundant structural proteins of the Bacillus subtilis spore outer-coat layer were used as carriers for the display of recombinant proteins, only one convincing example resulted in the display of functional enzymes. In addition, no examples are available about the use of an inner-coat protein for the display of an active passenger enzyme. In our study, we show that the inner-coat oxalate decarboxylase (OxdD) can expose an endogenous phytase, a commonly used feed enzyme for monogastric animals, in an active form at the spore surface. Importantly, despite the higher abundance of CotG outer-coat protein, an OxdD-Phy fusion was more represented at the spore surface. The potential of OxdD as a carrier protein is further documented through the spore display of a bioactive heterologous passenger, the tetrameric beta-glucuronidase enzyme from Escherichia coli.

Indexed as

6-PhytaseBacillus subtilisBacterial ProteinsBiotechnologyCarboxy-LyasesCarrier ProteinsEscherichia coli ProteinsGenetic EngineeringGlucuronidaseMembrane ProteinsRecombinant ProteinsSpores, Bacterial6-PhytaseBacterial ProteinsCarboxy-LyasesCarrier ProteinsEscherichia coli ProteinsGlucuronidaseMembrane Proteinsoxalate decarboxylaseRecombinant Proteins

Identifiers

PMID20601499
PMCPMC2935070
OpenAlexW2143164469

What OpenQuestion holds

Textmetadata
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.