Evidence map›Paper›PMID 29737275›Full record

ArticleParasite (Paris, France)2018

Metallopeptidases of Toxoplasma gondii: in silico identification and gene expression.

Sandie Escotte-Binet, Antoine Huguenin, Dominique Aubert, Anne-Pascaline Martin, Matthieu Kaltenbach, Isabelle Florent, Isabelle Villena

Open access · goldAbstract read
In one paragraph

Article in Parasite (Paris, France), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. 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 3 institutions in 1 country.

Sandie Escotte-BinetEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France - Laboratory of Parasitology-Mycology, Toxoplasmosis National Reference Center, Toxoplasma Biological Resource Center, Maison Blanche Hospital, 51100 Reims, France.
Antoine HugueninEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France - Laboratory of Parasitology-Mycology, Toxoplasmosis National Reference Center, Toxoplasma Biological Resource Center, Maison Blanche Hospital, 51100 Reims, France.
Dominique AubertEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France - Laboratory of Parasitology-Mycology, Toxoplasmosis National Reference Center, Toxoplasma Biological Resource Center, Maison Blanche Hospital, 51100 Reims, France.
Anne-Pascaline MartinEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France.
Matthieu KaltenbachEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France.
Isabelle FlorentUMR7245 CNRS-MNHN, National Museum of Natural History, Department Adaptations of the Living, 75005 Paris, France.
Isabelle VillenaEA 7510, ESCAPE, Laboratory of Parasitology-Mycology, University of Reims Champagne-Ardenne, 51100 Reims, France - Laboratory of Parasitology-Mycology, Toxoplasmosis National Reference Center, Toxoplasma Biological Resource Center, Maison Blanche Hospital, 51100 Reims, France.
Centre Hospitalier Universitaire de Reims · FREpidémiosurveillance et circulation des parasites dans les environnements · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metallopeptidases are a family of proteins with domains that remain highly conserved throughout evolution. These hydrolases require divalent metal cation(s) to activate the water molecule in order to carry out their catalytic action on peptide bonds by nucleophilic attack. Metallopeptidases from parasitic protozoa, including Toxoplasma, are investigated because of their crucial role in parasite biology. In the present study, we screened the T. gondii database using PFAM motifs specific for metallopeptidases in association with the MEROPS peptidase Database (release 10.0). In all, 49 genes encoding proteins with metallopeptidase signatures were identified in the Toxoplasma genome. An Interpro Search enabled us to uncover their domain/motif organization, and orthologs with the highest similarity by BLAST were used for annotation. These 49 Toxoplasma metallopeptidases clustered into 15 families described in the MEROPS database. Experimental expression analysis of their genes in the tachyzoite stage revealed transcription for all genes studied. Further research on the role of these peptidases should increase our knowledge of basic Toxoplasma biology and provide opportunities to identify novel therapeutic targets. This type of study would also open a path towards the comparative biology of apicomplexans.

Indexed as

Gene ExpressionGenome, ProtozoanAmino Acid SequenceAnimalsComputer SimulationLife Cycle StagesMetalloproteasesToxoplasmaMetalloproteases

Identifiers

PMID29737275
PMCPMC5939537
OpenAlexW2802996846

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.