Evidence map›Paper›PMID 33557917›Full record

ArticleParasites & vectors2021

Molecular characterization and expression analysis of annexin B3 and B38 as secretory proteins in Echinococcus granulosus.

Hongyu Song, Xue He, Xiaodi Du, Ruiqi Hua, Jing Xu, Ran He, Yue Xie, Xiaobin Gu, Xuerong Peng, Guangyou Yang

Open access · goldAbstract read
In one paragraph

Article in Parasites & vectors, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.8field-weighted citation impact, top 16% 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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3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 13 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

10 authors at 1 institution in 1 country.

Hongyu SongDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xue HeDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xiaodi DuDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Ruiqi HuaDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Jing XuDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Ran HeDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Yue XieDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xiaobin GuDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China.
Xuerong PengDepartment of Chemistry, College of Life and Basic Science, Sichuan Agricultural University, Wenjiang, 611130, China.
Guangyou YangDepartment of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Wenjiang, 611130, China. guangyou1963@aliyun.com.
Sichuan Agricultural University · CN

Funding

the Key TechnologyR&D Program of Sichuan Province, China No. 2020YFN0030the National Natural Science Foundation of China No. 31672547
6 · The paper itself

Abstract

backgroundCystic echinococcosis is a parasitic zoonotic disease, which poses a threat to public health and animal husbandry, and causes significant economic losses. Annexins are a family of phospholipid-binding proteins with calcium ion-binding activity, which have many functions.

methodsTwo annexin protein family genes [Echinococcus granulosus annexin B3 (EgAnxB3) and EgAnxB38] were cloned and molecularly characterized using bioinformatic analysis. The immunoreactivity of recombinant EgAnxB3 (rEgAnxB3) and rEgAnxB38 was investigated using western blotting. The distribution of EgAnxB3 and EgAnxB38 in protoscoleces (PSCs), the germinal layer, 18-day strobilated worms and 45-day adult worms was analyzed by immunofluorescence localization, and their secretory characteristics were analyzed preliminarily; in addition, quantitative real-time reverse transcription polymerase chain reaction was used to analyze their transcript levels in PSCs and 28-day strobilated worms stages. The phospholipid-binding activities of rEgAnxB3 and rEgAnxB38 were also analyzed.

resultsEgAnxB3 and EgAnxB38 are conserved and contain calcium-binding sites. Both rEgAnxB3 and rEgAnxB38 could be specifically recognized by the serum samples from E. granulosus-infected sheep, indicating that they had strong immunoreactivity. EgAnxB3 and EgAnxB38 were distributed in all stages of E. granulosus, and their transcript levels were high in the 28-day strobilated worms. They were found in liver tissues near the cysts. In addition, rEgAnxB3 has Ca

conclusionsEgAnxB3 and EgAnxB38 contain calcium-binding sites, and rEgAnxB3 has Ca

Indexed as

Amino Acid SequenceAnimalsAnnexinsCloning, MolecularComputational BiologyDogsEchinococcosisEchinococcus granulosusFemaleMaleProtein BindingRabbitsSequence AlignmentSheepAnnexinsAnnexinCalcium ionEchinococcus granulosusImmunofluorescence localizationSecretory proteinWestern blotting

Identifiers

PMID33557917
PMCPMC7869467
OpenAlexW3118191592

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.