Evidence map›Paper›PMID 30136251›Full record

ArticleArchives of virology2018

Characterization of influenza A virus pseudotyped with the spike protein of porcine epidemic diarrhea virus.

Asawin Wanitchang, Janya Saenboonrueng, Kanjana Srisutthisamphan, Anan Jongkaewwattana

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. The Alpha-1 Subunit of the NaInternational journal of molecular sciences · 2023
    Article
  3. Article
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 1 institution in 1 country.

Asawin WanitchangVirology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Nation Science and Technology Development Agency (NSTDA), 113 Thailand Science Park, Phahonyothin Rd., Klong 1, Klong Luang, Pathum Thani, 12120, Thailand.
Janya SaenboonruengVirology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Nation Science and Technology Development Agency (NSTDA), 113 Thailand Science Park, Phahonyothin Rd., Klong 1, Klong Luang, Pathum Thani, 12120, Thailand.
Kanjana SrisutthisamphanVirology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Nation Science and Technology Development Agency (NSTDA), 113 Thailand Science Park, Phahonyothin Rd., Klong 1, Klong Luang, Pathum Thani, 12120, Thailand.
Anan JongkaewwattanaVirology and Cell Technology Laboratory, National Center for Genetic Engineering and Biotechnology (BIOTEC), Nation Science and Technology Development Agency (NSTDA), 113 Thailand Science Park, Phahonyothin Rd., Klong 1, Klong Luang, Pathum Thani, 12120, Thailand. anan.jon@biotec.or.th.ORCID http://orcid.org/0000-0003-2354-9883
National Science and Technology Development Agency · TH

Funding

National Science and Technology Development Agency P15-51261
6 · The paper itself

Abstract

The coronavirus spike protein and the influenza virus hemagglutinin are class I viral membrane fusion proteins. While the two proteins display strong structural conservation and the mechanisms underlying membrane fusion are similar, they share no sequence similarity. Whether they are functionally interchangeable is currently unknown. In this study, we constructed scIAV-S, a single-cycle influenza A virus pseudotyped with the spike protein of porcine epidemic diarrhea virus (PEDV), and demonstrated that this virus could infect cultured cells and trigger massive syncytium formation. Treatment with endocytosis inhibitors did not affect syncytium formation by infected cells. Moreover, the infectivity of scIAV-S was associated with the degree of cell adaptation of PEDV-S. Intriguingly, scIAV-S lacking functional neuraminidase (NA) exhibited substantially higher infectivity, suggesting a pivotal role of the sialic acid in the binding/entry of PEDV. Together, scIAV-S offers a robust platform for the investigation of the entry mechanism of PEDV or, possibly, of other coronaviruses.

Indexed as

AnimalsCell LineCoronavirus InfectionsInfluenza A virusPorcine epidemic diarrhea virusRecombinant Fusion ProteinsSpike Glycoprotein, CoronavirusSwineSwine DiseasesRecombinant Fusion ProteinsSpike Glycoprotein, Coronavirus

Identifiers

PMID30136251
PMCPMC7087185
OpenAlexW2888659845

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.