Evidence map›Paper›PMID 32891183›Full record

ArticleVeterinary research2020

Molecular cloning and characterization of a novel peptidase from Trichinella spiralis and protective immunity elicited by the peptidase in BALB/c mice.

Jun Jun Lei, Yuan Yuan Hu, Fang Liu, Shu Wei Yan, Ruo Dan Liu, Shao Rong Long, Peng Jiang, Jing Cui, Zhong Quan Wang

Open access · goldAbstract read
In one paragraph

Article in Veterinary research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.7field-weighted citation impact, top 17% 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

30 citing papers in PubMed, 57 citations in OpenAlex.

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  9. Repurposing of Amiodarone for treatment of muscle phase of experimental trichinellosis spiralis.Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2025
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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.

Jun Jun LeiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Yuan Yuan HuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Fang LiuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Shu Wei YanDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Ruo Dan LiuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Shao Rong LongDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Peng JiangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Jing CuiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. cuij@zzu.edu.cn.ORCID http://orcid.org/0000-0001-8726-5498
Zhong Quan WangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. wangzq2015@126.com.
Zhengzhou University · CN

Funding

National Major Science and Technology Projects of China (CN) 81971952National Natural Science Foundation of China 81871673
6 · The paper itself

Abstract

In our previous studies, a novel T. spiralis peptidase (TsP) was identified among the excretory/secretory (ES) proteins of T. spiralis intestinal infective larvae (IIL) and T. spiralis at the adult worm (AW) stage using immunoproteomics, but the biological function of TsP in the life cycle of T. spiralis is not clear. The objective of this study was to investigate the biological properties and functions of TsP in larval intrusion and protective immunity induced by immunization with rTsP. The complete TsP cDNA sequence was cloned and expressed. The results of RT-PCR, indirect immunofluorescence assay (IIFA) and western blotting revealed that TsP is a surface and secretory protein expressed in T. spiralis at different stages (muscle larvae, IIL, AWs and newborn larvae) that is principally localized at the epicuticle of the nematode. rTsP facilitated the larval intrusion of intestinal epithelial cells (IECs) and intestinal mucosa, whereas anti-rTsP antibodies suppressed larval intrusion; these facilitative and suppressive roles were dose-dependently related to rTsP or anti-rTsP antibodies. Immunization of mice with rTsP triggered an obvious humoral immune response (high levels of IgG, IgG1/IgG2a, and sIgA) and also elicited systemic (spleen) and intestinal local mucosal (mesenteric lymph node) cellular immune responses, as demonstrated by an evident increase in the cytokines IFN-γ and IL-4. Immunization of mice with rTsP reduced the numbers of intestinal adult worms by 38.6% and muscle larvae by 41.93%. These results demonstrate that TsP plays a vital role in the intrusion, development and survival of T. spiralis in hosts and is a promising candidate target molecule for anti-Trichinella vaccines.

Indexed as

AnimalsFemaleHelminth ProteinsImmunizationMiceMice, Inbred BALB CPeptide HydrolasesTrichinella spiralisVaccinesHelminth ProteinsPeptide HydrolasesVaccinesintestinal epithelial cells (IECs)intrusionpeptidaseprotective immunityTrichinella spiralis

Identifiers

PMID32891183
PMCPMC7487599
OpenAlexW3083644208

What OpenQuestion holds

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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.