Evidence map›Paper›PMID 32461314›Full record

ArticleJournal of virology2020

A Genetically Engineered Rotavirus NSP2 Phosphorylation Mutant Impaired in Viroplasm Formation and Replication Shows an Early Interaction between vNSP2 and Cellular Lipid Droplets.

Jeanette M Criglar, Sue E Crawford, Boyang Zhao, Hunter G Smith, Fabio Stossi, Mary K Estes

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.7field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

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  9. Rotavirus-mediated DGAT1 degradation: A pathophysiological mechanism of viral-induced malabsorptive diarrhea.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 1 institution in 1 country.

Jeanette M CriglarDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Sue E CrawfordDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Boyang ZhaoDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Hunter G SmithDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA.
Fabio StossiDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas, USA.
Mary K EstesDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA mestes@bcm.edu.
Baylor College of Medicine · US

Funding

Tumor BiologyP30CA125123 · NCI · BAYLOR COLLEGE OF MEDICINE · PI Michael M Ittmann · 2007 to 2026
$73.9M
Tissue Analysis & Molecular Imaging CoreP30DK056338 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI James Versalovic · 2001 to 2026
$28.3M
Translational Research Support CoreP30ES030285 · NIEHS · BAYLOR COLLEGE OF MEDICINE · PI Casey W Wright · 2019 to 2026
$14.7M
Regulation of Rotavirus ReplicationR01AI080656 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI Sue Ellen Crawford, Mary Kolb Estes · 2009 to 2026
$7.9M
Regulation of Rotavirus ReplicationR56AI080656 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI ESTES, MARY KOLB · 2014 to 2014
$433k
NCI NIH HHS P30 CA125123NIAID NIH HHS R01 AI080656NIAID NIH HHS R56 AI080656NIDDK NIH HHS P30 DK056338NIEHS NIH HHS P30 ES030285
6 · The paper itself

Abstract

Many RNA viruses replicate in cytoplasmic compartments (virus factories or viroplasms) composed of viral and cellular proteins, but the mechanisms required for their formation remain largely unknown. Rotavirus (RV) replication in viroplasms requires interactions between virus nonstructural proteins NSP2 and NSP5, which are associated with components of lipid droplets (LDs). We previously identified two forms of NSP2 in RV-infected cells, a cytoplasmically dispersed form (dNSP2) and a viroplasm-specific form (vNSP2), which interact with hypophosphorylated and hyperphosphorylated NSP5, respectively, indicating that a coordinated phosphorylation cascade controls viroplasm assembly. The cellular kinase CK1α phosphorylates NSP2 on serine 313, triggering the localization of vNSP2 to sites of viroplasm assembly and its association with hyperphosphorylated NSP5. Using reverse genetics, we generated a rotavirus with a phosphomimetic NSP2 (S313D) mutation to directly evaluate the role of CK1α NSP2 phosphorylation in viroplasm formation. Recombinant rotavirus NSP2 S313D (rRV NSP2 S313D) is significantly delayed in viroplasm formation and in virus replication and interferes with wild-type RV replication in coinfection. Taking advantage of the delay in viroplasm formation, the NSP2 phosphomimetic mutant was used as a tool to observe very early events in viroplasm assembly. We show that (i) viroplasm assembly correlates with NSP5 hyperphosphorylation and (ii) vNSP2 S313D colocalizes with RV-induced LDs without NSP5, suggesting that vNSP2 phospho-S313 is sufficient for interacting with LDs and may be the virus factor required for RV-induced LD formation. Further studies with the rRV NSP2 S313D virus are expected to reveal new aspects of viroplasm and LD initiation and assembly.

Indexed as

AnimalsCell LineCricetinaeLipid DropletsPhosphorylationRNA-Binding ProteinsRotavirusViral Nonstructural ProteinsVirus ReplicationNS35 protein, rotavirusRNA-Binding ProteinsViral Nonstructural ProteinsCK1αlipid dropletNSP2NSP5perilipinPLIN1protein phosphorylationreplicationrotavirusviroplasm

Identifiers

PMID32461314
PMCPMC7375380
OpenAlexW3032086730

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.