Evidence map›Paper›PMID 33230237›Full record

ArticleScientific reports2020

Comparative analyses and structural insights of new class glutathione transferases in Cryptosporidium species.

Mbalenhle Sizamile Mfeka, José Martínez-Oyanedel, Wanping Chen, Ikechukwu Achilonu, Khajamohiddin Syed, Thandeka Khoza

Open access · goldAbstract readComparative Study
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Caseinolytic Proteins (Clp) in the GenusMolecules (Basel, Switzerland) · 2021
    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 5 institutions in 3 countries.

Mbalenhle Sizamile MfekaDepartment of Biochemistry, School of Life Sciences, University of KwaZulu-Natal (Pietermaritzburg Campus), Scottsville, Pietermaritzburg, KwaZulu-Natal, 3209, South Africa.
José Martínez-OyanedelLaboratorio de Biofísica Molecular, Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Barrio Universitario S/N, Casilla 160_C, Concepción, Chile.
Wanping ChenDepartment of Molecular Microbiology and Genetics, University of Göttingen, 37077, Göttingen, Germany.
Ikechukwu AchilonuProtein Structure-Function Research Unit, School of Molecular and Cell Biology, University of the Witwatersrand, Braamfontein, Johannesburg, South Africa.
Khajamohiddin SyedDepartment of Biochemistry and Microbiology, Faculty of Science and Agriculture, University of Zululand, 1 Main Road Vulindlela, KwaDlangezwa, 3886, South Africa. khajamohiddinsyed@gmail.com.
Thandeka KhozaDepartment of Biochemistry, School of Life Sciences, University of KwaZulu-Natal (Pietermaritzburg Campus), Scottsville, Pietermaritzburg, KwaZulu-Natal, 3209, South Africa. khozat1@ukzn.ac.za.
University of KwaZulu-Natal · ZAUniversity of Concepción · CLUniversity of Göttingen · DEUniversity of the Witwatersrand · ZAUniversity of Zululand · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryptosporidiosis, caused by protozoan parasites of the genus Cryptosporidium, is estimated to rank as a leading cause in the global burden of neglected zoonotic parasitic diseases. This diarrheal disease is the second leading cause of death in children under 5 years of age. Based on the C. parvum transcriptome data, glutathione transferase (GST) has been suggested as a drug target against this pathogen. GSTs are diverse multifunctional proteins involved in cellular defense and detoxification in organisms and help pathogens to alleviate chemical and environmental stress. In this study, we performed genome-wide data mining, identification, classification and in silico structural analysis of GSTs in fifteen Cryptosporidium species. The study revealed the presence three GSTs in each of the Cryptosporidium species analyzed in the study. Based on the percentage identity and comprehensive comparative phylogenetic analysis, we assigned Cryptosporidium species GSTs to three new GST classes, named Vega (ϑ), Gamma (γ) and Psi (ψ). The study also revealed an atypical thioredoxin-like fold in the C. parvum GST1 of the Vega class, whereas C. parvum GST2 of the Gamma class and C. melagridis GST3 of the Psi class has a typical thioredoxin-like fold in the N-terminal region. This study reports the first comparative analysis of GSTs in Cryptosporidium species.

Indexed as

Amino Acid SequenceAnimalsCryptosporidiosisCryptosporidiumData MiningGlutathione TransferaseHumansModels, MolecularPhylogenyProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein FoldingProtein Interaction Domains and MotifsProtozoan ProteinsSequence AlignmentStructural Homology, ProteinGlutathione TransferaseProtozoan ProteinsThioredoxins

Identifiers

PMID33230237
PMCPMC7683740
OpenAlexW3109555932

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.