Evidence map›Paper›PMID 16149915›Full record

ArticleThe Biochemical journal2005

Role for a P-type H+-ATPase in the acidification of the endocytic pathway of Trypanosoma cruzi.

Mauricio Vieira, Peter Rohloff, Shuhong Luo, Narcisa L Cunha-e-Silva, Wanderley de Souza, Roberto Docampo

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2005. 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
1.4field-weighted citation impact, top 19% 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, 42 citations in OpenAlex.

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  15. Reservosomes: multipurpose organelles?Parasitology research · 2006
    Review
  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

6 authors at 1 institution in 1 country.

Mauricio VieiraLaboratory of Molecular Parasitology, Department of Pathobiology and Center for Zoonoses Research, University of Illinois at Urbana-Champaign, Urbana, IL 61802, U.S.A.
Peter Rohloff
Shuhong Luo
Narcisa L Cunha-e-Silva
Wanderley de Souza
Roberto Docampo
Universidade Federal do Rio de Janeiro · BR

Funding

UIUC COLLEGE VET MED COMPLETION SHELL SPACEC06RR016515 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WHITELEY, HERBERT E · 2001 to 2001
$1.5M
MODE OF ACTION TRYPANOCIDAL DRUGS--INVOLVEMENT OF CA++R01AI023259 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI DOCAMPO, ROBERTO · 1987 to 2002
$1.1M
Acidocalcisomes in Trypanosoma cruziR21AI023259 · NIAID · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI DOCAMPO, ROBERTO · 2003 to 2003
$383k
NCRR NIH HHS C06 RR016515NCRR NIH HHS C06 RR16515-01NIAID NIH HHS AI-23259NIAID NIH HHS R01 AI023259NIAID NIH HHS R21 AI023259
6 · The paper itself

Abstract

Previous studies in Trypanosoma cruzi, the etiologic agent of Chagas disease, have resulted in the cloning and sequencing of a pair of tandemly linked genes (TcHA1 and TcHA2) that encode P (phospho-intermediate form)-type H+-ATPases with homology to fungal and plant proton-pumping ATPases. In the present study, we demonstrate that these pumps are present in the plasma membrane and intracellular compartments of three different stages of T. cruzi. The main intracellular compartment containing these ATPases in epimastigotes was identified as the reservosome. This identification was achieved by immunofluorescence assays and immunoelectron microscopy showing their co-localization with cruzipain, and by subcellular fractionation and detection of their activity. ATP-dependent proton transport by isolated reservosomes was sensitive to vanadate and insensitive to bafilomycin A1, which is in agreement with the localization of P-type H+-ATPases in these organelles. Analysis by confocal immunofluorescence microscopy revealed that epitope-tagged TcHA1-Ty1 and TcHA2-Ty1 gene products are localized in the reservosomes, whereas the TcHA1-Ty1 gene product is additionally present in the plasma membrane. Immunogold electron microscopy showed the presence of the H+-ATPases in other compartments of the endocytic pathway such as the cytostome and endosomal vesicles, suggesting that in contrast with most cells investigated until now, the endocytic pathway of T. cruzi is acidified by a P-type H+-ATPase.

Indexed as

EndocytosisAnimalsCell MembraneEndosomesGene Expression Regulation, EnzymologicHydrogen-Ion ConcentrationProtein TransportProtonsProton-Translocating ATPasesProtozoan ProteinsTrypanosoma cruziHA1 protein, Trypanosoma cruziHA2 protein, Trypanosoma cruziProtonsProton-Translocating ATPasesProtozoan Proteins

Identifiers

PMID16149915
PMCPMC1316285
OpenAlexW1982644990

What OpenQuestion holds

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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.