Evidence map›Paper›PMID 27605674›Full record

ArticleJournal of virology2016

Alteration of a Second Putative Fusion Peptide of Structural Glycoprotein E2 of Classical Swine Fever Virus Alters Virus Replication and Virulence in Swine.

L G Holinka, E Largo, D P Gladue, V O'Donnell, G R Risatti, J L Nieva, M V Borca

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.6field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

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  8. The EViruses · 2021
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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

7 authors at 3 institutions in 2 countries.

L G HolinkaARS, USDA, Plum Island Animal Disease Center, Greenport, New York, USA.
E LargoBiophysics Unit (CSIC, UPV/EHU), Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Bilbao, Spain.
D P GladueARS, USDA, Plum Island Animal Disease Center, Greenport, New York, USA.
V O'DonnellARS, USDA, Plum Island Animal Disease Center, Greenport, New York, USA.
G R RisattiDepartment of Pathobiology and Veterinary Science, CANR, University of Connecticut, Storrs, Connecticut, USA.
J L NievaBiophysics Unit (CSIC, UPV/EHU), Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), Bilbao, Spain.
M V BorcaARS, USDA, Plum Island Animal Disease Center, Greenport, New York, USA manuel.borca@ars.usda.gov.
Plum Island Animal Disease Center · USUniversity of the Basque Country · ESUniversity of Connecticut · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E2, the major envelope glycoprotein of classical swine fever virus (CSFV), is involved in several critical virus functions, including cell attachment, host range susceptibility, and virulence in natural hosts. Functional structural analysis of E2 based on a Wimley-White interfacial hydrophobicity distribution predicted the involvement of a loop (residues 864 to 881) stabilized by a disulfide bond ( IMPORTANCE: This report describes the identification and characterization of a putative fusion peptide (FP) in the major structural protein E2 of classical swine fever virus (CSFV). The FP identification was performed by functional structural analysis of E2. We characterized the functional significance of this FP by using artificial membranes. Replacement of critical amino acid residues within the FP radically alters how it interacts with the artificial membranes. When we introduced the same mutations into the viral sequence, there was a reduction in replication in cell cultures, and when we infected domestic swine, the natural host of CSFV host, we observed that the virus was now completely attenuated in swine. In addition, the virus mutant that was attenuated in vivo efficiently protected pigs against wild-type virus. These results provide the proof of principle to support as a strategy for vaccine development the discovery and manipulation of FPs.

Indexed as

Amino Acid SubstitutionAnimalsCell LineClassical Swine FeverClassical Swine Fever VirusGlycoproteinsIntercellular Signaling Peptides and ProteinsMutationPeptidesSwineViral Envelope ProteinsVirulenceVirus ReplicationGlycoproteinsIntercellular Signaling Peptides and ProteinsPeptidesstructural-GP protein, Bos taurusViral Envelope Proteins

Identifiers

PMID27605674
PMCPMC5105664
OpenAlexW2508320949

What OpenQuestion holds

Textmetadata
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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.