Evidence map›Paper›PMID 22500103›Full record

ArticleJournal of biomedicine & biotechnology2012

EhADH112 is a Bro1 domain-containing protein involved in the Entamoeba histolytica multivesicular bodies pathway.

Cecilia Bañuelos, Guillermina García-Rivera, Israel López-Reyes, Leobardo Mendoza, Arturo González-Robles, Silvia Herranz, Olivier Vincent, Esther Orozco

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomedicine & biotechnology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. The CRISPR-Cas9 System inMicroorganisms · 2025
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  8. Molecular interplays of theFrontiers in cellular and infection microbiology · 2022
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  9. Article
  10. Protein Sumoylation Is Crucial for Phagocytosis inInternational journal of molecular sciences · 2021
    Article
  11. Article
  12. Lipids inFrontiers in cellular and infection microbiology · 2020
    Review
  13. Review
  14. The Conserved ESCRT-III Machinery Participates in the Phagocytosis ofFrontiers in cellular and infection microbiology · 2018
    Article
  15. Epithelial Cells Expressing EhADH, AnFrontiers in cellular and infection microbiology · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. The cell surface proteome of Entamoeba histolytica.Molecular & cellular proteomics : MCP · 2014
    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

8 authors at 4 institutions in 2 countries.

Cecilia BañuelosDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional, México, DF, Mexico.
Guillermina García-Rivera
Israel López-Reyes
Leobardo Mendoza
Arturo González-Robles
Silvia Herranz
Olivier Vincent
Esther Orozco
Center for Research and Advanced Studies of the National Polytechnic Institute · MXInstituto de Investigaciones Biomédicas Sols-Morreale · ESInstituto Politécnico Nacional · MXUniversidad del Distrito Federal · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EhADH112 is an Entamoeba histolytica Bro1 domain-containing protein, structurally related to mammalian ALIX and yeast BRO1, both involved in the Endosomal Sorting Complexes Required for Transport (ESCRT)-mediated multivesicular bodies (MVB) biogenesis. Here, we investigated an alternative role for EhADH112 in the MVB protein trafficking pathway by overexpressing 166 amino acids of its N-terminal Bro1 domain in trophozoites. Trophozoites displayed diminished phagocytosis rates and accumulated exogenous Bro1 at cytoplasmic vesicles which aggregated into aberrant complexes at late stages of phagocytosis, probably preventing EhADH112 function. Additionally, the existence of a putative E. histolytica ESCRT-III subunit (EhVps32) presumably interacting with EhADH112, led us to perform pull-down experiments with GST-EhVps32 and [(35)S]-labeled EhADH112 or EhADH112 derivatives, confirming EhVps32 binding to EhADH112 through its Bro1 domain. Our overall results define EhADH112 as a novel member of ESCRT-accessory proteins transiently present at cellular surface and endosomal compartments, probably contributing to MVB formation during phagocytosis.

Indexed as

Adhesins, BacterialCalcium-Binding ProteinsCell Cycle ProteinsCell MembraneEndosomal Sorting Complexes Required for TransportEntamoeba histolyticaHistocytochemistryHumansModels, MolecularPhagocytosisProtozoan ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsTrophozoitesAdhesins, BacterialBro1 protein, S cerevisiaeCalcium-Binding ProteinsCell Cycle ProteinsEhADH112 protein, Entamoeba histolyticaEndosomal Sorting Complexes Required for TransportPDCD6IP protein, humanProtozoan ProteinsRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID22500103
PMCPMC3303925
OpenAlexW2065100982

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.