Evidence map›Paper›PMID 22069760›Full record

ArticleToxins2011

Modified heat-stable toxins (hSTa) of enterotoxigenic Escherichia coli lose toxicity but display antigenicity after being genetically fused to heat-labile toxoid LT(R192G).

Mei Liu, Chengxian Zhang, Kristy Mateo, James P Nataro, Donald C Robertson, Weiping Zhang

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Recent progress in enterotoxigenicInfection and immunity · 2025
    Review
  3. Article
  4. Review
  5. Coupling enterotoxigenic Escherichia coli heat-stable peptide toxin with 8-arm PEG enhances immunogenicity.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  6. Article
  7. Article
  8. Development of an enterotoxigenicHuman vaccines & immunotherapeutics · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. 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 1 country.

Mei LiuVeterinary & Biomedical Sciences Department, The Center for Infectious Disease Research & Vaccinology, South Dakota State University, Brookings, SD 57007, USA. mei.liu@sdstate.edu
Chengxian Zhang
Kristy Mateo
James P Nataro
Donald C Robertson
Weiping Zhang
South Dakota State University · USKansas State University · USUniversity of Virginia · US

Funding

Determining vaccine candidacy of LT and STa toxoid fusions against enterotoxigeniR21AI083897 · NIAID · SOUTH DAKOTA STATE UNIVERSITY · PI ZHANG, WEIPING · 2009 to 2010
$368k
NIAID NIH HHS AI083897NIAID NIH HHS R21 AI083897
6 · The paper itself

Abstract

Enterotoxigenic Escherichia coli (ETEC) strains are a major cause of diarrhea in humans and animals. Heat-stable (STa) and heat-labile (LT) enterotoxins produced by ETEC disrupt fluid homeostasis in host small intestinal epithelial cells and cause fluid and electrolyte hyper-secretion that leads to diarrhea. ETEC strains producing STa or LT are sufficiently virulent to cause diarrhea, therefore STa and LT antigens must be included in ETEC vaccines. However, potent toxicity and poor immunogenicity (of STa) prevent them from being directly applied as vaccine components. While LT toxoids, especially LT(R192G), being used in vaccine development, STa toxoids have not been included. A recent study (IAI, 78:316-325) demonstrated porcine-type STa toxoids [pSTa(P12F) and pSTa(A13Q)] elicited protective anti-STa antibodies after being fused to a porcine-type LT toxoid [pLT(R192G)]. In this study, we substituted the 8th, 9th, 16th, or the 17th amino acid of a human-type STa (hSTa) and generated 28 modified STa peptides. We tested each STa peptide for toxicity and structure integrity, and found nearly all modified STa proteins showed structure alteration and toxicity reduction. Based on structure similarity and toxic activity, three modified STa peptides: STa(E8A), STa(T16Q) and STa(G17S), were selected to construct LT(192)-STa(-toxoid) fusions. Constructed fusions were used to immunize mice, and immunized mice developed anti-STa antibodies. Results from this study provide useful information in developing toxoid vaccines against ETEC diarrhea.

Indexed as

AnimalsAntibodiesAntigensBacterial ToxinsEnterotoxigenic Escherichia coliEnterotoxinsEscherichia coli InfectionsEscherichia coli ProteinsEscherichia coli VaccinesFemaleIntestinal MucosaIntestinesMiceMice, Inbred BALB CPeptidesRecombinant Fusion ProteinsAntibodiesAntigensBacterial ToxinsEnterotoxinsEscherichia coli ProteinsEscherichia coli Vaccinesheat-labile enterotoxin, E coliheat stable toxin (E coli)PeptidesRecombinant Fusion ProteinsdiarrheaETECLT-STa toxoid fusionSTa toxintoxoidvaccine

Identifiers

PMID22069760
PMCPMC3202872
OpenAlexW2060831170

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.