Evidence map›Paper›PMID 17567921›Full record

ArticleBMC genomics2007

The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes.

Manuela Tillack, Laura Biller, Henriette Irmer, Michelle Freitas, Maria A Gomes, Egbert Tannich, Iris Bruchhaus

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 87 citations in OpenAlex.

  1. Amoebae: beyond pathogens- exploring their benefits and future potential.Frontiers in cellular and infection microbiology · 2024
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  5. Taxon-Specific Proteins of the PathogenicFrontiers in cellular and infection microbiology · 2021
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  6. The delicate balance betweenGut microbes · 2020
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  9. The American journal of tropical medicine and hygiene · 2018
    Article
  10. Cysteine proteases in protozoan parasites.PLoS neglected tropical diseases · 2018
    Review
  11. Article
  12. Environmental adaptation ofInternational journal of biological sciences · 2018
    Article
  13. Article
  14. Article
  15. Review
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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

7 authors at 2 institutions in 2 countries.

Manuela TillackBernhard Nocht Institute for Tropical Medicine, Hamburg, Germany. tillack@bni-hamburg.de <tillack@bni-hamburg.de>
Laura Biller
Henriette Irmer
Michelle Freitas
Maria A Gomes
Egbert Tannich
Iris Bruchhaus
Bernhard Nocht Institute for Tropical Medicine · DEUniversidade Federal de Minas Gerais · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundA number of studies have shown that peptidases and in particular cysteine peptidases constitute major pathogenicity factors in Entamoeba histolytica. Recent studies have suggested that a considerable number of genes coding for proteolytic enzymes are present within the E. histolytica genome and questions remain about the mode of expression of the various molecules.

resultsBy homology search within the recently published amoeba genome, we identified a total of 86 E. histolytica genes coding for putative peptidases, including 46 recently described peptidase genes. In total these comprise (i) 50 cysteine peptidases of different families but most of which belong to the C1 papain superfamily, (ii) 22 different metallo peptidases from at least 11 different families, (iii) 10 serine peptidases belonging to 3 different families, and (iv) 4 aspartic peptidases of only one family. Using an oligonucleotide microarray, peptidase gene expression patterns of 7 different E. histolytica isolates as well as of heat stressed cells were analysed. A total of 21 out of 79 amoeba peptidase genes analysed were found to be significantly expressed under standard axenic culture conditions whereas the remaining are not expressed or at very low levels only. In heat-stressed cells the expression of 2 and 3 peptidase genes, respectively, were either decreased or increased. Only minor differences were observed between the various isolates investigated, despite the fact that these isolates were originated from asymptomatic individuals or from patients with various forms of amoebic diseases.

conclusionEntamoeba histolytica possesses a large number of genes coding for proteolytic enzymes. Under standard culture conditions or upon heat-stress only a relatively small number of these genes is significantly expressed and only very few variations become apparent between various clinical E. histolytica isolates, calling into question the importance of these enzymes in E. histolytica pathogenicity. Further studies are required to define the precise role of most of the proteolytic enzyme for amoeba cell biology but in particular for E. histolytica virulence.

Indexed as

AnimalsBase SequenceComputational BiologyDatabases, Nucleic AcidEntamoeba histolyticaGene Expression ProfilingGenome, ProtozoanHot TemperatureOligonucleotide Array Sequence AnalysisPeptide HydrolasesPeptide Hydrolases

Identifiers

PMID17567921
PMCPMC1913524
OpenAlexW2074788196

What OpenQuestion holds

Textmetadata
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.