Evidence map›Paper›PMID 32339171›Full record

ArticlePLoS neglected tropical diseases2020

Molecular characterization of a Trichinella spiralis aspartic protease and its facilitation role in larval invasion of host intestinal epithelial cells.

Jia Xu, Ruo Dan Liu, Sheng Jie Bai, Hui Nan Hao, Wen Wen Yue, Yang Xiu Yue Xu, Shao Rong Long, Jing Cui, Zhong Quan Wang

Open access · goldAbstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.1field-weighted citation impact, top 12% 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

39 citing papers in PubMed, 69 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.

Jia XuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Ruo Dan LiuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Sheng Jie BaiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Hui Nan HaoDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Wen Wen YueDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Yang Xiu Yue XuDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.ORCID 0000-0001-6941-9609
Shao Rong LongDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Jing CuiDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.ORCID 0000-0001-8726-5498
Zhong Quan WangDepartment of Parasitology, Medical College, Zhengzhou University, Zhengzhou, PR China.
Zhengzhou University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundT. spiralis aspartic protease has been identified in excretion/secretion (ES) proteins, but its roles in larval invasion are unclear. The aim of this study was to characterize T. spiralis aspartic protease-2 (TsASP2) and assess its roles in T. spiralis invasion into intestinal epithelial cells (IECs) using RNAi. METHODOLOGY/PRINCIPAL

findingsRecombinant TsASP2 (rTsASP2) was expressed and purified. The native TsASP2 of 43 kDa was recognized by anti-rTsASP2 serum in all worm stages except newborn larvae (NBL), and qPCR indicated that TsASP2 transcription was highest at the stage of intestinal infective larvae (IIL). IFA results confirmed that TsASP2 was located in the hindgut, midgut and muscle cells of muscle larvae (ML) and IIL and intrauterine embryos of the female adult worm (AW), but not in NBL. rTsASP2 cleaved several host proteins (human hemoglobin (Hb), mouse Hb, collagen and IgM). The proteolytic activity of rTsASP2 was host-specific, as it hydrolyzed mouse Hb more efficiently than human Hb. The enzymatic activity of rTsASP2 was significantly inhibited by pepstatin A. The expression levels of TsASP2 mRNA and protein were significantly suppressed by RNAi with 5 μM TsASP2-specific siRNA. Native aspartic protease activity in ML crude proteins was reduced to 54.82% after transfection with siRNA. Larval invasion of IECs was promoted by rTsASP2 and inhibited by anti-rTsASP2 serum and siRNA. Furthermore, cell monolayer damage due to larval invasion was obviously alleviated when siRNA-treated larvae were used. The adult worm burden, length of adult worms and female fecundity were clearly reduced in mice challenged using siRNA-treated ML relative to the PBS group.

conclusionsrTsASP2 possesses the enzymatic activity of native aspartic protease and facilitates T. spiralis invasion of host IECs.

Indexed as

EndocytosisAnimalsAspartic Acid ProteasesDisease Models, AnimalEpithelial CellsGene Expression ProfilingHemoglobinsHumansImmunohistochemistryMice, Inbred BALB CParasite LoadProteolysisReal-Time Polymerase Chain ReactionTrichinella spiralisTrichinellosisAspartic Acid ProteasesHemoglobins

Identifiers

PMID32339171
PMCPMC7205320
OpenAlexW3019679406

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.