Evidence map›Paper›PMID 25790467›Full record

ArticlePloS one2015

Development and characterization of recombinant antibody fragments that recognize and neutralize in vitro Stx2 toxin from Shiga toxin-producing Escherichia coli.

Daniela Luz, Gang Chen, Andrea Q Maranhão, Leticia B Rocha, Sachdev Sidhu, Roxane M F Piazza

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.1field-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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Recent Advancements in Technologies to Detect EnterohaemorrhagicJournal of microbiology and biotechnology · 2023
    Review
  5. Therapeutic Antibodies Against Shiga Toxins: Trends and Perspectives.Frontiers in cellular and infection microbiology · 2022
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Treatment Strategies for Infections With Shiga Toxin-ProducingFrontiers in cellular and infection microbiology · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Diarrheagenic Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2016
    Review
  18. Review
  19. 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

6 authors at 3 institutions in 2 countries.

Daniela LuzLaboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil.
Gang ChenBanting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.
Andrea Q MaranhãoLaboratório de Imunologia, Universidade de Brasília, Brasília, Brazil.
Leticia B RochaLaboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil.
Sachdev SidhuBanting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Canada.
Roxane M F PiazzaLaboratório de Bacteriologia, Instituto Butantan, São Paulo, Brazil.
Instituto Butantan · BRUniversity of Toronto · CAUniversidade de Brasília · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStx toxin is a member of the AB5 family of bacterial toxins: the active A subunit has N-glycosidase activity against 28S rRNA, resulting in inhibition of protein synthesis in eukaryotic cells, and the pentamer ligand B subunits (StxB) bind to globotria(tetra)osylceramide receptors (Gb3/Gb4) on the cell membrane. Shiga toxin-producing Escherichia coli strains (STEC) may produce Stx1 and/or Stx2 and variants. Strains carrying Stx2 are considered more virulent and related to the majority of outbreaks, besides being usually associated with hemolytic uremic syndrome in humans. The development of tools for the detection and/or neutralization of these toxins is a turning point for early diagnosis and therapeutics. Antibodies are an excellent paradigm for the design of high-affinity, protein-based binding reagents used for these purposes. METHODS AND

findingsIn this work, we developed two recombinant antibodies; scFv fragments from mouse hybridomas and Fab fragments by phage display technology using a human synthetic antibody library. Both fragments showed high binding affinity to Stx2, and they were able to bind specifically to the GKIEFSKYNEDDTF region of the Stx2 B subunit and to neutralize in vitro the cytotoxicity of the toxin up to 80%. Furthermore, the scFv fragments showed 79% sensitivity and 100% specificity in detecting STEC strains by ELISA.

conclusionIn this work, we developed and characterized two recombinant antibodies against Stx2, as promising tools to be used in diagnosis or therapeutic approaches against STEC, and for the first time, we showed a human monovalent molecule, produced in bacteria, able to neutralize the cytotoxicity of Stx2 in vitro.

Indexed as

AnimalsAntibodies, NeutralizingCell LineHumansHybridomasImmunoglobulin Fab FragmentsMicePeptide LibrarySensitivity and SpecificityShiga-Toxigenic Escherichia coliShiga Toxin 2Single-Chain AntibodiesAntibodies, NeutralizingImmunoglobulin Fab FragmentsPeptide LibraryShiga Toxin 2Single-Chain Antibodies

Identifiers

PMID25790467
PMCPMC4366190
OpenAlexW1973104483

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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.