Evidence map›Paper›PMID 21135101›Full record

ArticleThe Journal of biological chemistry2011

Functional diversity of heat-labile toxins (LT) produced by enterotoxigenic Escherichia coli: differential enzymatic and immunological activities of LT1 (hLT) AND LT4 (pLT).

Juliana F Rodrigues, Camila Mathias-Santos, Maria Elisabete Sbrogio-Almeida, Jaime H Amorim, Joaquim Cabrera-Crespo, Andrea Balan, Luís C S Ferreira

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 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
0.4field-weighted citation impact, top 35% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Streptococcus mutans glutamate binding protein (GlnH) as antigen target for a mucosal anti-caries vaccine.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022
    Article
  6. The evolutionary diversification of theFrontiers in microbiology · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Diarrheagenic Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  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

7 authors at 4 institutions in 2 countries.

Juliana F RodriguesDepartment of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo 05508-000, Brazil.
Camila Mathias-Santos
Maria Elisabete Sbrogio-Almeida
Jaime H Amorim
Joaquim Cabrera-Crespo
Andrea Balan
Luís C S Ferreira
Institute of Biomedical Science · GBInstituto Butantan · BRUniversidade de São Paulo · BRBrazilian Biosciences National Laboratory · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat-labile toxins (LTs) have ADP-ribosylation activity and induce the secretory diarrhea caused by enterotoxigenic Escherichia coli (ETEC) strains in different mammalian hosts. LTs also act as adjuvants following delivery via mucosal, parenteral, or transcutaneous routes. Previously we have shown that LT produced by human-derived ETEC strains encompass a group of 16 polymorphic variants, including the reference toxin (LT1 or hLT) produced by the H10407 strain and one variant that is found mainly among bacterial strains isolated from pigs (LT4 or pLT). Herein, we show that LT4 (with six polymorphic sites in the A (K4R, K213E, and N238D) and B (S4T, A46E, and E102K) subunits) displays differential in vitro toxicity and in vivo adjuvant activities compared with LT1. One in vitro generated LT mutant (LTK4R), in which the lysine at position 4 of the A subunit was replaced by arginine, showed most of the LT4 features with an ∼10-fold reduction of the cytotonic effects, ADP-ribosylation activity, and accumulation of intracellular cAMP in Y1 cells. Molecular dynamic studies of the A subunit showed that the K4R replacement reduces the N-terminal region flexibility and decreases the catalytic site crevice. Noticeably, LT4 showed a stronger Th1-biased adjuvant activity with regard to LT1, particularly concerning activation of cytotoxic CD8(+) T lymphocytes when delivered via the intranasal route. Our results further emphasize the relevance of LT polymorphism among human-derived ETEC strains that may impact both the pathogenicity of the bacterial strain and the use of these toxins as potential vaccine adjuvants.

Indexed as

Adjuvants, ImmunologicAmino Acid SubstitutionAnimalsBacterial ToxinsCD8-Positive T-LymphocytesCell Line, TumorCyclic AMPEnterotoxigenic Escherichia coliEnterotoxinsEscherichia coli ProteinsFemaleHumansMiceMutation, MissensePolymorphism, GeneticSpecies SpecificityAdjuvants, ImmunologicBacterial ToxinsCyclic AMPEnterotoxinsEscherichia coli Proteinsheat-labile enterotoxin, E coli

Identifiers

PMID21135101
PMCPMC3037635
OpenAlexW1965875359

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.