Evidence map›Paper›PMID 34031713›Full record

ArticleParasitology research2021

Identification of an enolase gene and its physiological role in Spirometra mansoni.

Pei Liang, Xiuji Cui, Ruijia Fu, Peng Liang, Gang Lu, Dayong Wang

Abstract read
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In one paragraph

Article in Parasitology research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Pei LiangLaboratory of Biotechnology and Molecular Pharmacology, School of Life and Pharmaceutical Sciences, Hainan University, Haikou, 570228, Hainan, China.ORCID https://orcid.org/0000-0003-1674-8745
Xiuji CuiKey Laboratory of Tropical Translational Medicine of the Ministry of Education of China, Hainan Medical College, Haikou, 571199, Hainan, China.
Ruijia FuLaboratory of Biotechnology and Molecular Pharmacology, School of Life and Pharmaceutical Sciences, Hainan University, Haikou, 570228, Hainan, China.
Peng LiangSchool of Tropical Medicine and Laboratory Medicine, Hainan Medical College, Haikou, 571199, Hainan, China.
Gang LuKey Laboratory of Tropical Translational Medicine of the Ministry of Education of China, Hainan Medical College, Haikou, 571199, Hainan, China.
Dayong WangLaboratory of Biotechnology and Molecular Pharmacology, School of Life and Pharmaceutical Sciences, Hainan University, Haikou, 570228, Hainan, China. wangdy@hainanu.edu.cn.ORCID http://orcid.org/0000-0002-2086-1663
Hainan University · CNHainan Medical University · CN

Funding

the Education Department of Hainan Province Hnky2018-43the National Natural Science Foundation of China 31760246the National Natural Science Foundation of China 81560332the Natural Science Foundation of Hainan Province 814298the Program of Hainan Association for Science and Technology Plan to Youth R&D Innovation QCXM201918
6 · The paper itself

Abstract

Enolase is a crucial enzyme involved in the glycolytic pathway and gluconeogenesis in parasites. It also has been reported to function as a plasminogen receptor and may be involved in tissue invasion. In this study, the biochemical properties of the enolase of Spirometra mansoni (Smenolase) were investigated. The Smenolase gene was found to cluster closely with the enolase genes of Clonorchis sinensis and Echinococcus granulosus, and some functional motifs were identified as conserved. Smenolase was confirmed to be a component of the secretory/excretory products (ESPs) and a circulating antigen of spargana. Recombinant Smenolase expressed in vitro was able to bind to human plasminogen. Smenolase was detected in the eggs, testicles, and vitellaria of adult worms and the tegument of spargana. The transcription level of Smenolase was highest at the gravid proglottid stage. When spargana were cultured with glucose of different concentration in vitro, it was observed that the expression levels of Smenolase in the low-glucose groups were consistent with that of Smenolase in vivo. These results indicate that Smenolase is a critical enzyme involved in supplying energy to support the development and reproduction of the parasite, and it may also play a role in sparganum invasion.

Indexed as

AnimalsAntigens, HelminthEnergy MetabolismGene Expression Regulation, DevelopmentalHelminth ProteinsHumansPhosphopyruvate HydratasePlasminogenSparganumSpirometraAntigens, HelminthHelminth ProteinsPhosphopyruvate HydratasePlasminogenEnergy supplyEnolasePlasminogen receptorSecretory/excretory productsSpirometra mansoni

Identifiers

PMID34031713
OpenAlexW3164137222

What OpenQuestion holds

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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.