Evidence map›Paper›PMID 18070902›Full record

ArticleInfection and immunity2008

Immunogenic and plasminogen-binding surface-associated alpha-enolase of Trichomonas vaginalis.

V Mundodi, A S Kucknoor, J F Alderete

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2008. 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
3.0field-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

44 citing papers in PubMed, 99 citations in OpenAlex.

  1. Surface enolase is a virulence factor ofFrontiers in microbiology · 2026
    Article
  2. Review
  3. Article
  4. Structural Characterization ofPathogens (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Advancing Prevention of STIs by Developing Specific Serodiagnostic Targets:International journal of environmental research and public health · 2020
    Article
  7. Review
  8. Why Do Intravascular Schistosomes Coat Themselves in Glycolytic Enzymes?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019
    Article
  9. Article
  10. Review
  11. Review
  12. Serodiagnostic Potential of Alpha-Enolase FromFrontiers in microbiology · 2018
    Article
  13. Recombinant Enolase ofJournal of immunology research · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

V MundodiDepartment of Microbiology and Immunology, University of Texas Health Science Center, San Antonio, Texas 78229-3900, USA.
A S Kucknoor
J F Alderete
The University of Texas Health Science Center at San Antonio · US

Funding

San Antonio STI TM CRCU19AI045429 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BASEMAN, JOEL BARRY · 1999 to 2010
$13.9M
Trichomonas vaginalis: Molecular Analysis of AdherenceR01AI043940 · NIAID · WASHINGTON STATE UNIVERSITY · PI ALDERETE, JOHN F · 1999 to 2007
$1.4M
Trichomonas vaginalis Genetic Analysis of Cell AdherenceR21AI043940 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI ALDERETE, JOHN F · 2003 to 2003
$245k
NIAID NIH HHS AI43940NIAID NIH HHS AI45429NIAID NIH HHS R01 AI043940NIAID NIH HHS R21 AI043940NIAID NIH HHS U19 AI045429
6 · The paper itself

Abstract

Trichomonas vaginalis is a protist that causes the most common human sexually transmitted infection. A T. vaginalis cDNA expression library was screened with pooled sera from patients with trichomoniasis. A highly reactive cDNA clone of 1,428 bp encoded a trichomonad protein of 472 amino acids with sequence identity to alpha-enolase (tv-eno1). The sequence alignment confirmed the highly conserved nature of the enzyme with 65% to 84% identity among organisms. The expression of tv-eno1 was up-regulated by contact of parasites with vaginal epithelial cells, and this is the first report demonstrating up-regulation by cytoadherence of a plasminogen-binding alpha-enolase in T. vaginalis. Immunofluorescence with monoclonal antibody of nonpermeabilized trichomonads showed tv-ENO1 on the surface. The recombinant tv-ENO1 was expressed in Escherichia coli as a glutathione S-transferase (GST)::tv-ENO1 fusion protein, which was cleaved using thrombin to obtain affinity-purified recombinant tv-ENO1 protein (tv-rENO1) detectable in immunoblots by sera of patients. Immobilized tv-rENO1 bound human plasminogen in a dose-dependent manner, and plasminogen binding by tv-rENO1 was confirmed in a ligand blot assay. The plasminogen-specific inhibitor epsilon-aminocaproic acid blocked the tv-rENO1-plasminogen association, indicating that lysines play a role in binding to tv-rENO1. Further, both parasites and tv-rENO1 activate plasminogen to plasmin that is mediated by tissue plasminogen activator. These data indicate that as with other bacterial pathogens, tv-ENO1 is an anchorless, surface-associated glycolytic enzyme of T. vaginalis.

Indexed as

AnimalsAntibodies, ProtozoanAntigens, ProtozoanCloning, MolecularEpithelial CellsEscherichia coliGene ExpressionGene Expression RegulationGene LibraryHumansMembrane ProteinsPhosphopyruvate HydratasePlasminogenProtozoan ProteinsRecombinant ProteinsTrichomonas vaginalisAntibodies, ProtozoanAntigens, ProtozoanMembrane ProteinsPhosphopyruvate HydratasePlasminogenProtozoan ProteinsRecombinant Proteins

Identifiers

PMID18070902
PMCPMC2223476
OpenAlexW2136280219

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.