Evidence map›Paper›PMID 18158858›Full record

ArticleBMC microbiology2007

Characterization of the Trichomonas vaginalis surface-associated AP65 and binding domain interacting with trichomonads and host cells.

Ana F Garcia, Jf Alderete

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Microscopic and molecular detection ofFrontiers in microbiology · 2024
    Article
  7. Aptamer-Based Technologies for Parasite Detection.Sensors (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. A secreted Heat shock protein 90 of Trichomonas vaginalis.PLoS neglected tropical diseases · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  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

2 authors at 2 institutions in 1 country.

Ana F GarciaDepartment of Microbiology, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA. anafgarcia01@yahoo.com
Jf Alderete
The University of Texas Health Science Center at San Antonio · USWashington State University · US

Funding

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 R01 AI043940NIAID NIH HHS R21 AI043940
6 · The paper itself

Abstract

backgroundAP65 is a prominent adhesin of Trichomonas vaginalis that mediates binding of parasites to host vaginal epithelial cells (VECs). AP65 with no secretion signal sequence, membrane targeting peptide, and anchoring motif was recently found to be secreted.

resultsWe first wanted to demonstrate surface association of AP65 to the parasite followed by the identification of the binding epitope interacting with both organisms and VECs. AP65 was found to bind to trichomonads, but not to trypsin-treated parasites, in an auto-ligand assay, suggesting the existence of a surface protein associating with AP65. Since rabbit antiserum IgG antibodies reactive with epitopes localized to the N-terminal region of AP65 inhibit the attachment of live parasites to VECs, we hypothesized that the binding domain was localized to this region. We subcloned five overlapping fragments of AP65 called c1 through c5, and expression of recombinant clones was confirmed with antibodies to AP65. Each purified recombinant protein was then tested for binding activity using an established ligand assay, and fragment c1 with the first twenty-five amino acids in the N-terminal domain was required for binding to VECs and, surprisingly, also to parasites. Importantly, c1 competed with the binding of AP65 to both cells types.

conclusionT. vaginalis AP65 is a secreted, surface-associated protein and a model is proposed to explain how this secreted protein functions as an adhesin.

Indexed as

AnimalsCell AdhesionCell Adhesion MoleculesEpithelial CellsEpitopesFemaleHumansMembrane ProteinsProtein Structure, TertiaryProtozoan ProteinsRecombinant ProteinsTrichomonas vaginalisTrypsinVaginaCell Adhesion MoleculesEpitopesMembrane ProteinsProtozoan ProteinsRecombinant ProteinsTrypsin

Identifiers

PMID18158858
PMCPMC2222631
OpenAlexW2006722956

What OpenQuestion holds

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LicenceCC BY
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.