Evidence map›Paper›PMID 32539772›Full record

ArticleVeterinary research2020

Characterization of a Trichinella spiralis aminopeptidase and its participation in invasion, development and fecundity.

Kai Xia Guo, Ying Bai, Hua Nan Ren, Xiang Yuan Sun, Yan Yan Song, Ruo Dan Liu, Shao Rong Long, Xi Zhang, Peng Jiang, Zhong Quan Wang and 1 more

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.3field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 79 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

11 authors at 1 institution in 1 country.

Kai Xia GuoDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Ying BaiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Hua Nan RenDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Xiang Yuan SunDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Yan Yan SongDepartment 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.
Xi ZhangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Peng JiangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China.
Zhong Quan WangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. wangzq2015@126.com.
Jing CuiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, 450052, China. cuij@zzu.edu.cn.ORCID http://orcid.org/0000-0001-8726-5498
Zhengzhou University · CN

Funding

National Natural Science Foundation of China 81871673National Natural Science Foundation of China U1704284
6 · The paper itself

Abstract

A Trichinella spiralis aminopeptidase (TsAP) has been identified in intestinal infectious larvae (IIL) and adult worms (AW), but its biological function in the T. spiralis life cycle is unknown. The aim of this study was to characterize TsAP and ascertain its functions in the invasion, development and fecundity of T. spiralis. Recombinant TsAP (rTsAP) was expressed and purified. rTsAP has strong immunogenicity. qPCR and western blotting show that TsAP was transcribed and expressed at all T. spiralis lifecycle stages, but the expression level of TsAP mRNA and proteins at IIL and AW stages was obviously higher than those in muscle larvae (ML) and newborn larvae (NBL). The IFT results reveal that TsAP was principally located at the cuticle and the intrauterine embryos of this nematode. rTsAP had the enzymatic activity of natural aminopeptidase to hydrolyze the substrate Leu-pNA with an optimal temperature of 50 °C and optimal pH of 8.0. rTsAP promoted the larval penetration into intestinal epithelial cells, whereas anti-rTsAP antibodies suppressed the larval intrusion; the promotion and suppression was dose-dependently related to rTsAP or anti-rTsAP antibodies. TsAP protein expression level and enzymatic activity were reduced by 50.90 and 49.72% through silencing of the TsAP gene by specific siRNA 842. Intestinal AW and muscle larval burdens, worm length and female reproductive capacity were significantly declined in mice infected with siRNA-transfected ML compared to the control siRNA and PBS group. These results indicate that TsAP participates in the invasion, development and fecundity of T. spiralis and it might be a candidate target for anti-Trichinella vaccines.

Indexed as

AminopeptidasesAnimalsFemaleFertilityHelminth ProteinsMiceMice, Inbred BALB CSus scrofaSwineSwine DiseasesTrichinella spiralisTrichinellosisAminopeptidasesHelminth Proteins

Identifiers

PMID32539772
PMCPMC7296678
OpenAlexW3034835114

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.