Evidence map›Paper›PMID 24416391›Full record

ArticlePloS one2014

Interaction of CSFV E2 protein with swine host factors as detected by yeast two-hybrid system.

Douglas P Gladue, Ryan Baker-Bransetter, Lauren G Holinka, Ignacio J Fernandez-Sainz, Vivian O'Donnell, Paige Fletcher, Zhiqiang Lu, Manuel V Borca

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
7.4field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

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  12. Identification of the linear ligand epitope on classical swine fever virus that interacts with porcine kidney 15 cells.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2017
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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

8 authors at 3 institutions in 1 country.

Douglas P GladuePlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America ; Department of Pathobiology and Veterinary Science, University of Connecticut, Storrs, Connecticut, United States of America.
Ryan Baker-BransetterPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America.
Lauren G HolinkaPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America.
Ignacio J Fernandez-SainzPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America.
Vivian O'DonnellPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America ; Department of Pathobiology and Veterinary Science, University of Connecticut, Storrs, Connecticut, United States of America.
Paige FletcherPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America.
Zhiqiang LuPlum Island Animal Disease Center, Department of Homeland Security, Greenport, New York, United States of America.
Manuel V BorcaPlum Island Animal Disease Center, Agriculture Research Service, United States Department of Agriculture, Greenport, New York, United States of America.
Plum Island Animal Disease Center · USUnited States Department of Agriculture · USUniversity of Connecticut · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E2 is one of the envelope glycoproteins of pestiviruses, including classical swine fever virus (CSFV) and bovine viral diarrhea virus (BVDV). E2 is involved in several critical functions, including virus entry into target cells, induction of a protective immune response and virulence in swine. However, there is no information regarding any host binding partners for the E2 proteins. Here, we utilized the yeast two-hybrid system and identified fifty-seven host proteins as positive binding partners which bound E2 from both CSFV and BVDV with the exception of two proteins that were found to be positive for binding only to CSFV E2. Alanine scanning of CSFV E2 demonstrated that the binding sites for these cellular proteins on E2 are likely non-linear binding sites. The possible roles of the identified host proteins are discussed as the results presented here will be important for future studies to elucidate mechanisms of host protein-virus interactions during pestivirus infection. However, due to the limitations of the yeast two hybrid system, the proteins identified is not exhaustive and each interaction identified needs to be confirmed by independent experimental approaches in the context of virus-infected cells before any definitive conclusion can be drawn on relevance for the virus life cycle.

Indexed as

Host-Pathogen InteractionsAmino Acid SequenceAnimalsBinding SitesBovine Virus Diarrhea-Mucosal DiseaseCattleClassical Swine FeverClassical Swine Fever VirusDiarrhea Viruses, Bovine ViralGene ExpressionGene LibraryMolecular Sequence AnnotationMolecular Sequence DataProtein BindingSequence AlignmentSwineglycoprotein E2, classical swine fever virusViral Envelope Proteins

Identifiers

PMID24416391
PMCPMC3885694
OpenAlexW2059009528

What OpenQuestion holds

Textmetadata
LicenceCC0
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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.