Evidence map›Paper›PMID 19270100›Full record

ArticleJournal of bacteriology2009

Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila.

Jian Sha, Tatiana E Erova, Rebecca A Alyea, Shaofei Wang, Juan P Olano, Vijay Pancholi, Ashok K Chopra

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Enolase ofFrontiers in microbiology · 2022
    Article
  7. Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021
    Review
  8. Article
  9. Review
  10. Article
  11. Population Genomic Analysis ofMicroorganisms · 2020
    Article
  12. Review
  13. An Update on the GenusMicroorganisms · 2020
    Review
  14. Article
  15. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  16. Article
  17. Review
  18. Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  19. Review
  20. Recombinant Enolase ofJournal of immunology research · 2018
    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 2 institutions in 2 countries.

Jian ShaDepartment of Microbiology and Immunology, Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, Texas 77555, USA.
Tatiana E Erova
Rebecca A Alyea
Shaofei Wang
Juan P Olano
Vijay Pancholi
Ashok K Chopra
The University of Texas Medical Branch at Galveston · USThe Ohio State University · US

Funding

Cytotoxic Enterotoxin in Aeromonas-mediated DiseasesR01AI041611 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI CHOPRA, ASHOK K · 1997 to 2006
$1.1M
NIAID NIH HHS AI041611NIAID NIH HHS R01 AI041611
6 · The paper itself

Abstract

In this study, we demonstrated that the surface-expressed enolase from diarrheal isolate SSU of Aeromonas hydrophila bound to human plasminogen and facilitated the latter's tissue-type plasminogen activator-mediated activation to plasmin. The bacterial surface-bound plasmin was more resistant to the action of its specific physiological inhibitor, the antiprotease alpha(2)-antiplasmin. We found that immunization of mice with purified recombinant enolase significantly protected the animals against a lethal challenge dose of wild-type (WT) A. hydrophila. Minimal histological changes were noted in organs from mice immunized with enolase and then challenged with WT bacteria compared to severe pathological changes found in the infected and nonimmunized group of animals. This correlated with the smaller bacterial load of WT bacteria in the livers and spleens of enolase-immunized mice than that found in the nonimmunized controls. We also showed that the enolase gene could potentially be important for the viability of A. hydrophila SSU as we could delete the chromosomal copy of the enolase gene only when another copy of the targeted gene was supplied in trans. By site-directed mutagenesis, we altered five lysine residues located at positions 343, 394, 420, 427, and 430 of enolase in A. hydrophila SSU; the mutated forms of enolase were hyperexpressed in Escherichia coli, and the proteins were purified. Our results indicated that lysine residues at positions 420 and 427 of enolase were crucial in plasminogen-binding activity. We also identified a stretch of amino acid residues ((252)FYDAEKKEY(260)) in the A. hydrophila SSU enolase involved in plasminogen binding. To our knowledge, this is the first report of the direct involvement of surface-expressed enolase in the pathogenesis of A. hydrophila SSU infections and of any gram-negative bacteria in general.

Indexed as

Aeromonas hydrophilaAnimalsBacterial ProteinsBacterial VaccinesBinding SitesColony Count, MicrobialDiarrheaFibrinolysinGene DeletionGenes, BacterialGenes, EssentialGram-Negative Bacterial InfectionsHumansLiverMiceMicrobial ViabilityBacterial ProteinsBacterial VaccinesFibrinolysinPhosphopyruvate HydratasePlasminogenVirulence Factors

Identifiers

PMID19270100
PMCPMC2681796
OpenAlexW2159916948

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.