Evidence map›Paper›PMID 26131960›Full record

ReviewViruses2015

Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters.

Fun-In Wang, Ming-Chung Deng, Yu-Liang Huang, Chia-Yi Chang

Open access · goldAbstract readReview
In one paragraph

Review in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.8field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

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  12. Molecular characteristics of a potentially novel BVDV (Frontiers in veterinary science · 2025
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  13. Review
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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

4 authors at 2 institutions in 1 country.

Fun-In WangSchool of Veterinary Medicine, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei 10617, Taiwan. fiwangvm@ntu.edu.tw.
Ming-Chung DengAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, Taiwan. mcdeng@mail.nvri.gov.tw.
Yu-Liang HuangAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, Taiwan. ylhuang@mail.nvri.gov.tw.
Chia-Yi ChangAnimal Health Research Institute, Council of Agriculture, 376 Chung-Cheng Road, Tansui, New Taipei City 25158, Taiwan. cychang@mail.nvri.gov.tw.
Council of Agriculture · TWNational Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pestiviruses, which include economically important animal pathogens such as bovine viral diarrhea virus and classical swine fever virus, possess three envelope glycoproteins, namely Erns, E1, and E2. This article discusses the structures and functions of these glycoproteins and their effects on viral pathogenicity in cells in culture and in animal hosts. E2 is the most important structural protein as it interacts with cell surface receptors that determine cell tropism and induces neutralizing antibody and cytotoxic T-lymphocyte responses. All three glycoproteins are involved in virus attachment and entry into target cells. E1-E2 heterodimers are essential for viral entry and infectivity. Erns is unique because it possesses intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferons and assist in the development of persistent infections. These glycoproteins are localized to the virion surface; however, variations in amino acids and antigenic structures, disulfide bond formation, glycosylation, and RNase activity can ultimately affect the virulence of pestiviruses in animals. Along with mutations that are driven by selection pressure, antigenic differences in glycoproteins influence the efficacy of vaccines and determine the appropriateness of the vaccines that are currently being used in the field.

Indexed as

AnimalsCattleCattle DiseasesPestivirusPestivirus InfectionsSwineSwine DiseasesViral Envelope ProteinsVirus InternalizationViral Envelope ProteinsE1E2Ernsfunctionglycoproteinpestivirusstructure

Identifiers

PMID26131960
PMCPMC4517112
OpenAlexW1483895932

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.