Evidence map›Paper›PMID 27606705›Full record

ArticlePloS one2016

Development of Recombinant Lactococcus lactis Displaying Albumin-Binding Domain Variants against Shiga Toxin 1 B Subunit.

Petra Zadravec, Lucie Marečková, Hana Petroková, Vesna Hodnik, Milica Perišić Nanut, Gregor Anderluh, Borut Štrukelj, Petr Malý, Aleš Berlec

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. 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
2.9field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Treatment Strategies for Infections With Shiga Toxin-ProducingFrontiers in cellular and infection microbiology · 2020
    Review
  9. Article
  10. EngineeredMicroorganisms · 2019
    Article
  11. Review
  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

9 authors at 4 institutions in 2 countries.

Petra ZadravecDepartment of Biotechnology, Jožef Stefan Institute, Jamova 39, SI-1000, Ljubljana, Slovenia.
Lucie MarečkováLaboratory of Ligand Engineering, Institute of Biotechnology CAS, v. v. i., BIOCEV Research Center, Průmyslová 595, 252 50, Vestec, Czech Republic.
Hana PetrokováLaboratory of Ligand Engineering, Institute of Biotechnology CAS, v. v. i., BIOCEV Research Center, Průmyslová 595, 252 50, Vestec, Czech Republic.
Vesna HodnikDepartment of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia.
Milica Perišić NanutDepartment of Biotechnology, Jožef Stefan Institute, Jamova 39, SI-1000, Ljubljana, Slovenia.
Gregor AnderluhDepartment of Biology, Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000, Ljubljana, Slovenia.
Borut ŠtrukeljDepartment of Biotechnology, Jožef Stefan Institute, Jamova 39, SI-1000, Ljubljana, Slovenia.
Petr MalýLaboratory of Ligand Engineering, Institute of Biotechnology CAS, v. v. i., BIOCEV Research Center, Průmyslová 595, 252 50, Vestec, Czech Republic.
Aleš BerlecDepartment of Biotechnology, Jožef Stefan Institute, Jamova 39, SI-1000, Ljubljana, Slovenia.
Czech Academy of Sciences, Institute of Biotechnology · CZUniversity of Ljubljana · SIJožef Stefan Institute · SINational Institute of Chemistry · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infections with shiga toxin-producing bacteria, like enterohemorrhagic Escherichia coli and Shigella dysenteriae, represent a serious medical problem. No specific and effective treatment is available for patients with these infections, creating a need for the development of new therapies. Recombinant lactic acid bacterium Lactococcus lactis was engineered to bind Shiga toxin by displaying novel designed albumin binding domains (ABD) against Shiga toxin 1 B subunit (Stx1B) on their surface. Functional recombinant Stx1B was produced in Escherichia coli and used as a target for selection of 17 different ABD variants (named S1B) from the ABD scaffold-derived high-complex combinatorial library in combination with a five-round ribosome display. Two most promising S1Bs (S1B22 and S1B26) were characterized into more details by ELISA, surface plasmon resonance and microscale thermophoresis. Addition of S1Bs changed the subcellular distribution of Stx1B, completely eliminating it from Golgi apparatus most likely by interfering with its retrograde transport. All ABD variants were successfully displayed on the surface of L. lactis by fusing to the Usp45 secretion signal and to the peptidoglycan-binding C terminus of AcmA. Binding of Stx1B by engineered lactococcal cells was confirmed using flow cytometry and whole cell ELISA. Lactic acid bacteria prepared in this study are potentially useful for the removal of Shiga toxin from human intestine.

Indexed as

AlbuminsCell Surface Display TechniquesElectrophoresis, Polyacrylamide GelEnzyme-Linked Immunosorbent AssayFlow CytometryHeLa CellsHumansImmobilized ProteinsLactococcus lactisProtein BindingProtein DomainsProtein SubunitsProtein TransportRecombinant ProteinsRecombination, GeneticRibosomesAlbuminsImmobilized ProteinsProtein SubunitsRecombinant ProteinsShiga Toxin 1

Identifiers

PMID27606705
PMCPMC5015993
OpenAlexW2508362523

What OpenQuestion holds

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LicenceCC BY
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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.