Evidence map›Paper›PMID 36315477›Full record

ArticlePLoS neglected tropical diseases2022

Characterization of a novel pyruvate kinase from Trichinella spiralis and its participation in sugar metabolism, larval molting and development.

Wen Wen Yue, Shu Wei Yan, Ru Zhang, Yong Kang Cheng, Ruo Dan Liu, Shao Rong Long, Xi Zhang, Zhong Quan Wang, Jing Cui

Open access · goldAbstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Wen Wen YueDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Shu Wei YanDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Ru ZhangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Yong Kang ChengDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Ruo Dan LiuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Shao Rong LongDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Xi ZhangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Zhong Quan WangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.
Jing CuiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, People's Republic of China.ORCID 0000-0001-8726-5498
Zhengzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPyruvate kinase widely exists in many parasites and plays an important role in the energy production for the parasites. Pyruvate kinase might be a potential drug target for killing the parasites. The aim of the present study was to evaluate the biological characteristics and roles of T. spiralis pyruvate kinase M (TsPKM) in sugar metabolism, larval molting and development of T. spiralis. METHODOLOGY/PRINCIPAL

findingsTsPKM has two functional domains of pyruvate kinase and the tertiary structure of TsPKM is tetramer which has the enzyme active site constituted by 8 amino-acid residues (Arg71, Asn73, Asp110, Phe241, Lys267, Glu269, Asp293 and Thr325). Recombinant TsPKM (rTsPKM) was expressed and purified. The rTsPKM had good immunogenicity. RT-PCR and Western blot showed that TsPKM was transcribed and expressed at various developmental stages in T. spiralis lifecycle. Immunofluorescence test showed that TsPKM was principally located in the cuticle, muscle, stichosome, intestine and the intrauterine embryos of female adults. rTsPKM catalyzed the reaction of phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP) to produce pyruvic acid and adenosine triphosphate (ATP). TsPKM played an important role in the metabolism and energy production of T. spiralis. After silencing of TsPKM gene by specific dsRNA-TsPKM2, protein expression and enzyme activity of TsPKM decreased by 50.91 and 26.06%, respectively. After treatment with RNAi, natural TsPKM enzyme activity, larval molting, sugar metabolism, growth and development of T. spiralis were significantly reduced.

conclusionsTsPKM participates in the larval molting, sugar metabolism, growth and development of T. spiralis and it might be a candidate target of therapeutic drug of trichinellosis.

Indexed as

ParasitesTrichinella spiralisTrichinellosisAnimalsFemaleHelminth ProteinsLarvaMiceMice, Inbred BALB CMoltingPyruvate KinaseSugarsHelminth ProteinsPyruvate KinaseSugars

Identifiers

PMID36315477
PMCPMC9621426
OpenAlexW4307715494

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LicenceCC BY
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Registered trials

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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.