Evidence map›Paper›PMID 30013278›Full record

ArticleIndian journal of microbiology2018

Molecular Cloning and Identification of the 2'-5' Oligoadenylate Synthetase 2 Gene in Chinese Domestic Pigs Through Bioinformatics Analysis, and Determination of Its Antiviral Activity Against Porcine Reproductive and Respiratory Syndrome Virus Infection.

Ruining Wang, Hongfang Ma, Yinfeng Kang, Cunfa Li, Huawei Li, Erqin Zhang, Pengchao Ji, Jian He, Mengmeng Zhao

Open access · bronzeAbstract read
In one paragraph

Article in Indian journal of microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Article
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 3 institutions in 1 country.

Ruining Wang1School of Pharmaceutical Engineering, Henan University of Animal Husbandry and Economy, Zhengzhou, 450046 People's Republic of China.
Hongfang Ma2College of Animal Husbandry and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002 People's Republic of China.
Yinfeng Kang3State Key Laboratory of Oncology in South China, Department of Experimental Research, Collaborative Innovation Center for Cancer Medicine, Sun Yat-Sen University Cancer Center, Guangzhou, 467500 People's Republic of China.
Cunfa Li1School of Pharmaceutical Engineering, Henan University of Animal Husbandry and Economy, Zhengzhou, 450046 People's Republic of China.
Huawei Li4College of Biology Engineering, Henan University of Animal Husbandry and Economy, Zhengzhou, 450046 People's Republic of China.
Erqin Zhang2College of Animal Husbandry and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002 People's Republic of China.
Pengchao Ji2College of Animal Husbandry and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002 People's Republic of China.
Jian He2College of Animal Husbandry and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002 People's Republic of China.
Mengmeng Zhao2College of Animal Husbandry and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002 People's Republic of China.ORCID 0000-0002-6589-4100
Henan Agricultural University · CNHenan University · CNSun Yat-sen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An interferon-mediated antiviral protein, 2'-5' oligoadenylate synthetase 2, plays an important role in the antiviral response of interferons. In this study, 2'-5' oligoadenylate synthetase 2 genes were cloned from Chinese domestic pigs. Bioinformatics analysis revealed that the 2024-bp long open reading fame encodes 707 amino acids. There are two conserved regions in this protein: the nucleotidyltransferase domain, and the 2'-5' oligoadenylate synthetase domain (OAS). Genetic evolution analysis showed that the 2'-5' oligoadenylate synthetase 2 gene in domestic pigs is closely related to that of cattle. There are multiple antigenic sites, no signal peptide, and no transmembrane region in the gene, which is predicted to be a hydrophilic protein. Secondary structures were found to be mainly alpha helix-based; its tertiary structure is close to that of humans and cattle, but not that of mice. Tissue distribution results indicated that this protein is distributed in multiple organs, with high distribution in the liver; it is mainly localized in the cytoplasm. PRRSV infection, interferon-beta, and Poly(I: C) treatment all promoted 2'-5' oligoadenylate synthetase 2 gene expression. Overexpression and RNA silencing of porcine OAS2 inhibited and promoted PRRSV replication in cells, respectively. The inhibitory effect of porcine OAS2 was mainly dependent on RNase L, similar to what was predicted. This study has laid the foundation for future antiviral studies in pig, and provided a new way of preventing and treating PRRSV in the future.

Indexed as

2′–5′ Oligoadenylate synthetaseBioinformaticsPRRSVReplicationRNase L

Identifiers

PMID30013278
PMCPMC6023816
OpenAlexW2801453178

What OpenQuestion holds

Textmetadata
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.