Evidence map›Paper›PMID 25278143›Full record

ReviewVirus research2014

Membrane proteins of arterivirus particles: structure, topology, processing and function.

Michael Veit, Anna Karolina Matczuk, Balaji Chandrasekhar Sinhadri, Eberhard Krause, Bastian Thaa

Open access · bronzeAbstract readReview
In one paragraph

Review in Virus research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
6.5field-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

56 citing papers in PubMed, 77 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

5 authors at 2 institutions in 1 country.

Michael VeitInstitut für Virologie, Veterinärmedizin, Freie Universität Berlin, Germany. Electronic address: mveit@zedat.fu-berlin.de.
Anna Karolina MatczukInstitut für Virologie, Veterinärmedizin, Freie Universität Berlin, Germany.
Balaji Chandrasekhar SinhadriInstitut für Virologie, Veterinärmedizin, Freie Universität Berlin, Germany.
Eberhard KrauseLeibniz Institute of Molecular Pharmacology (FMP), Berlin, Germany.
Bastian ThaaInstitut für Virologie, Veterinärmedizin, Freie Universität Berlin, Germany.
Freie Universität Berlin · DELeibniz Association · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arteriviruses, such as equine arteritis virus (EAV) and porcine reproductive and respiratory syndrome virus (PRRSV), are important pathogens in veterinary medicine. Despite their limited genome size, arterivirus particles contain a multitude of membrane proteins, the Gp5/M and the Gp2/3/4 complex, the small and hydrophobic E protein and the ORF5a protein. Their function during virus entry and budding is understood only incompletely. We summarize current knowledge of their primary structure, membrane topology, (co-translational) processing and intracellular targeting to membranes of the exocytic pathway, which are the budding site. We profoundly describe experimental data that led to widely believed conceptions about the function of these proteins and also report new results about processing steps for each glycoprotein. Further, we depict the location and characteristics of epitopes in the membrane proteins since the late appearance of neutralizing antibodies may lead to persistence, a characteristic hallmark of arterivirus infection. Some molecular features of the arteriviral proteins are rare or even unique from a cell biological point of view, particularly the prevention of signal peptide cleavage by co-translational glycosylation, discovered in EAV-Gp3, and the efficient use of overlapping sequons for glycosylation. This article reviews the molecular mechanisms of these cellular processes. Based on this, we present hypotheses on the structure and variability of arteriviral membrane proteins and their role during virus entry and budding.

Indexed as

Protein Modification, TranslationalVirus InternalizationVirus ReleaseAntibodies, NeutralizingAntibodies, ViralEpitopesEquartevirusModels, BiologicalModels, MolecularPorcine respiratory and reproductive syndrome virusProtein ConformationProtein TransportViral Matrix ProteinsAntibodies, NeutralizingAntibodies, ViralEpitopesViral Matrix ProteinsArterivirusEquine arteritis virusGlycosylationMembrane topologyPorcine reproductive and respiratory syndrome virusSignal peptide

Identifiers

PMID25278143
PMCPMC7172906
OpenAlexW2027477169

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.