Evidence map›Paper›PMID 18086807›Full record

ArticleInfection and immunity2008

Participation of the serine-rich Entamoeba histolytica protein in amebic phagocytosis of apoptotic host cells.

Jose E Teixeira, Christopher D Huston

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 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Diversity and Plasticity of Virulent Characteristics ofTropical medicine and infectious disease · 2023
    Review
  3. Article
  4. Article
  5. Antigenic membrane proteins of virulent variant ofPathogens and global health · 2020
    Article
  6. Revisiting Drug Development Against the Neglected Tropical Disease, Amebiasis.Frontiers in cellular and infection microbiology · 2020
    Review
  7. Uncovering the Cyclic AMP Signaling Pathway of the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2020
    Article
  8. Article
  9. PeerJ · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Evolutionary genomics and population structure of Entamoeba histolytica.Computational and structural biotechnology journal · 2014
    Review
  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

2 authors at 1 institution in 1 country.

Jose E TeixeiraDepartment of Medicine, University of Vermont College of Medicine, Burlington, VT 05405, USA.
Christopher D Huston
University of Vermont · US

Funding

VERMONT IMMUNOBIOLOIGY/ INFECTIOUS DISEASES CENTERP20RR021905 · NCRR · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI HUSTON, CHRISTOPHER D · 2006 to 2011
$14.5M
E. histolytica phagocytosis of apoptotic host cellsK08AI053678 · NIAID · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI HUSTON, CHRISTOPHER D · 2003 to 2007
$649k
NCRR NIH HHS P20 RR021905NIAID NIH HHS K08 AI053678
6 · The paper itself

Abstract

Entamoeba histolytica is an intestinal ameba that causes dysentery and liver abscesses. Cytotoxicity and phagocytosis of host cells characterize invasive E. histolytica infection. Prior to phagocytosis of host cells, E. histolytica induces apoptotic host cell death, using a mechanism that requires contact via an amebic galactose-specific lectin. However, lectin inhibition only partially blocks phagocytosis of already dead cells, implicating at least one additional receptor in phagocytosis. To identify receptors for engulfment of apoptotic cells, monoclonal antibodies against E. histolytica membrane antigens were screened for inhibition of phagocytosis. Of 43 antibodies screened, one blocked lectin-independent uptake of apoptotic cells, with >90% inhibition at a dose of 20 microg/ml (P < 0.0003 versus control). The same antibody also inhibited adherence to apoptotic lymphocytes and, to a lesser extent, adherence to and killing of viable lymphocytes. The antigen recognized by the inhibitory antibody was purified by affinity chromatography and identified by liquid chromatography-mass spectrometry as the serine-rich E. histolytica protein (SREHP). Consistent with this, the inhibitory antibody bound to recombinant SREHP present in bacterial lysates on immunoblots. The SREHP is an abundant immunogenic surface protein of unclear function. The results of this unbiased antibody screen strongly implicate the SREHP as a participant in E. histolytica phagocytosis and suggest that it may play an important role in adherence to apoptotic cells.

Indexed as

PhagocytosisAnimalsAntibodies, MonoclonalAntibodies, ProtozoanCell AdhesionCell LineChromatography, AffinityEntamoeba histolyticaHumansMass SpectrometryMembrane ProteinsMicroscopy, ConfocalProtozoan ProteinsAntibodies, MonoclonalAntibodies, ProtozoanMembrane ProteinsProtozoan Proteinsserine-rich protein, Entamoeba histolytica

Identifiers

PMID18086807
PMCPMC2258814
OpenAlexW2152798475

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.