Evidence map›Paper›PMID 28962639›Full record

ArticleParasites & vectors2017

Cloning and expression of a Trichinella spiralis putative glutathione S-transferase and its elicited protective immunity against challenge infections.

Chun Ying Liu, Yan Yan Song, Hua Na Ren, Ge Ge Sun, Ruo Dan Liu, Peng Jiang, Shao Rong Long, Xi Zhang, Zhong Quan Wang, Jing Cui

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

35 citing papers in PubMed, 68 citations in OpenAlex.

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  16. Characterization of a Novel Glutamine Synthetase FromFrontiers in cell and developmental biology · 2021
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  17. 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

10 authors at 1 institution in 1 country.

Chun Ying LiuDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Yan Yan SongDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Hua Na RenDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Ge Ge SunDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Ruo Dan LiuDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Peng JiangDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Shao Rong LongDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Xi ZhangDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China.
Zhong Quan WangDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China. wangzq2015@126.com.
Jing CuiDepartment of Parasitology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou, 450052, China. cuij@zzu.edu.cn.
Zhengzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlutathione-S-transferase (GST) is a widespread multigene family of detoxification enzymes. The vaccination of mice with recombinant GST of 24 kDa from Trichinella spiralis elicited a low immune protection against challenge infection. The objective of this study was to characterize the T. spiralis putative GST gene (TspGST) encoding a 30.8 kDa protein and to evaluate its potential as a candidate antigen for anti-Trichinella vaccine.

methodsThe full-length cDNA sequence of TspGST from T. spiralis muscle larvae (ML) was expressed in E. coli. The enzymatic activity and antigenicity of the rTspGST were identified by spectrophotometry, Western blot, and ELISA. The expression of TspGST at T. spiralis various stages was investigated by RT-PCR and indirect immunofluorescent test (IIFT). Serum level of total IgG, IgG1, and IgG2a antibodies against rTspGST were measured by ELISA. The immune protection produced by vaccination with rTspGST against T. spiralis was evaluated.

resultsThe sequencing results showed that the cDNA of TspGST was 840 bp, and encoded a protein of 279 amino acids, which had a molecular size of 30.8 kDa and a pI of 5.21. Its amino acid sequence shares 37% similarity with TsGST. The rTspGST protein had enzymatic activity of GST. On Western blot and ELISA analysis, the native TspGST protein with 30.8 kDa in crude antigens derived from adult worms (AW), newborn larvae (NBL), infective intestinal larvae (IIL) and ML was recognized by anti-rTspGST sera, but the ML ES antigens could be not recognized by anti-rTspGST sera. Expression of TspGST was found in all of T. spiralis various stages (AW, NBL, ML, and IIL). An immunolocalization analysis identified TspGST in different stages (mainly in cuticles) of the nematode. The mice vaccinated with the rTspGST elicited Th2-predominant immune responses, showed a 34.38% reduction of adult worms and a 43.70% reduction of muscle larvae.

conclusionsImmunization with rTspGST produced a partial immune protection, and the rTspGST could be regarded as a potential candidate target for an anti-Trichinella vaccine.

Indexed as

Cloning, MolecularAnimalsAntibodies, HelminthFemaleGlutathione TransferaseHelminth ProteinsHumansMiceMice, Inbred BALB CTrichinella spiralisTrichinellosisVaccinesAntibodies, HelminthGlutathione TransferaseHelminth ProteinsVaccinesGlutathione-S-transferase (GST)MiceProtective immunityTrichinella spiralis

Identifiers

PMID28962639
PMCPMC5622431
OpenAlexW2759031121

What OpenQuestion holds

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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.