Evidence map›Paper›PMID 21840351›Full record

ArticleVirus research2011

Mutation in the cytoplasmic retrieval signal of porcine epidemic diarrhea virus spike (S) protein is responsible for enhanced fusion activity.

Kazuya Shirato, Madoka Maejima, Shutoku Matsuyama, Makoto Ujike, Ayako Miyazaki, Natsumi Takeyama, Hidetoshi Ikeda, Fumihiro Taguchi

Abstract read
In one paragraph

Article in Virus research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 29 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

8 authors at 4 institutions in 1 country.

Kazuya ShiratoLaboratory of Acute Respiratory Viral Diseases and Cytokines, Department of Virology III, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashimurayama, Tokyo 208-0011, Japan.
Madoka Maejima
Shutoku Matsuyama
Makoto Ujike
Ayako Miyazaki
Natsumi Takeyama
Hidetoshi Ikeda
Fumihiro Taguchi
National Institute of Infectious Diseases · JPNippon Veterinary and Life Science University · JPNational Institute of Animal Health · JPNippon Institute for Biological Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Murine-adapted porcine epidemic diarrhea virus (PEDV), MK-p10, shows high neurovirulence and increased fusion activity compared with a non-adapted MK strain. MK-p10 S protein had four mutations relative to the original virus S, and one of these (H→R at position 1381, H1381R) in the cytoplasmic tail (CT) was suggested to be responsible for the increased fusion activity. To explore this, we examined fusion activity using recombinant S proteins. We expressed and compared the fusion activity of MK-p10 S, S with the H1381R mutation, S with the three other mutations that were not thought to be involved in high fusion activity, and the original S protein. The MK-p10 and MK-H1381R S proteins induced larger cell fusions than others. We also examined the distribution of these S proteins; the MK-p10 and MK-H1381R S proteins were transported onto the cell surface more efficiently than others. These findings suggest that the H1381R mutation is responsible for enhanced fusion activity, which may be attributed to the efficient transfer of S onto the cell surface. H1381 is a component of the KxHxx motif in the CT region, which is a retrieval signal of the S protein for the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). Loss of this motif could allow for the efficient transfer of S proteins from ERGIC onto the cell surface and subsequent increased fusion activity.

Indexed as

Mutation, MissenseProtein Sorting SignalsVirus InternalizationAmino Acid SequenceAnimalsCell LineCoronavirus InfectionsCytoplasmMembrane GlycoproteinsMolecular Sequence DataPorcine epidemic diarrhea virusProtein TransportSpike Glycoprotein, CoronavirusSwineSwine DiseasesViral Envelope ProteinsMembrane GlycoproteinsProtein Sorting SignalsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, mouse hepatitis virusViral Envelope Proteins

Identifiers

PMID21840351
PMCPMC7114372
OpenAlexW2042223278

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.