Evidence map›Paper›PMID 36598201›Full record

ArticleJournal of virology2023

N-Glycosylation of Rotavirus NSP4 Protein Affects Viral Replication and Pathogenesis.

Jeffery A Nurdin, Tomohiro Kotaki, Takahiro Kawagishi, Shintaro Sato, Moeko Yamasaki, Ryotaro Nouda, Shohei Minami, Yuta Kanai, Takeshi Kobayashi

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 23 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

9 authors at 2 institutions in 1 country.

Jeffery A Nurdin *Department of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Tomohiro Kotaki *Department of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Takahiro KawagishiDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Shintaro SatoDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0001-5156-3354
Moeko YamasakiDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Ryotaro NoudaDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Shohei MinamiDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0002-3999-348X
Yuta KanaiDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Takeshi KobayashiDepartment of Virology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0002-5532-207X
The University of Osaka · JPOsaka International Cancer Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rotavirus (RV), the most common cause of gastroenteritis in children, carries a high economic and health burden worldwide. RV encodes six structural proteins and six nonstructural proteins (NSPs) that play different roles in viral replication. NSP4, a multifunctional protein involved in various viral replication processes, has two conserved N-glycosylation sites; however, the role of glycans remains elusive. Here, we used recombinant viruses generated by a reverse genetics system to determine the role of NSP4 N-glycosylation during viral replication and pathogenesis. The growth rate of recombinant viruses that lost one glycosylation site was as high as that of the wild-type virus. However, a recombinant virus that lost both glycosylation sites (glycosylation-defective virus) showed attenuated replication in cultured cell lines. Specifically, replications of glycosylation-defective virus in MA104 and HT29 cells were 10- and 100,000-fold lower, respectively, than that of the wild-type, suggesting that N-glycosylation of NSP4 plays a critical role in RV replication. The glycosylation-defective virus showed NSP4 mislocalization, delay of cytosolic Ca

Indexed as

RotavirusRotavirus InfectionsViral Nonstructural ProteinsVirus ReplicationAnimalsGastroenteritisGlycosylationMiceToxins, BiologicalNS28 protein, rotavirusToxins, BiologicalViral Nonstructural ProteinsN-glycosylationNSP4rotavirusviral replication

Identifiers

PMID36598201
PMCPMC9888287
OpenAlexW4313477288

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.