Evidence map›Paper›PMID 30381491›Full record

ArticleJournal of virology2019

Components of the Reovirus Capsid Differentially Contribute to Stability.

Anthony J Snyder, Joseph Che-Yen Wang, Pranav Danthi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Energy Requirements for Loss of Viral Infectivity.Food and environmental virology · 2020
    Article
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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

3 authors at 1 institution in 1 country.

Anthony J SnyderDepartment of Biology, Indiana University, Bloomington, Indiana, USA.ORCID 0000-0002-2551-9461
Joseph Che-Yen WangElectron Microscopy Center, Indiana University, Bloomington, Indiana, USA.
Pranav DanthiDepartment of Biology, Indiana University, Bloomington, Indiana, USA pdanthi@indiana.edu.ORCID 0000-0001-6199-6022
Indiana University Bloomington · US

Funding

Regulating the Detection of Reovirus InfectionR01AI110637 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Pranav Danthi · 2014 to 2026
$4.5M
Characterizing the Role of Specific Host Lipids during Reovirus Cell EntryF32AI126643 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI SNYDER, ANTHONY J · 2017 to 2018
$124k
NIAID NIH HHS F32 AI126643NIAID NIH HHS R01 AI110637
6 · The paper itself

Abstract

The mammalian orthoreovirus (reovirus) outer capsid is composed of 200 μ1-σ3 heterohexamers and a maximum of 12 σ1 trimers. During cell entry, σ3 is degraded by luminal or intracellular proteases to generate the infectious subviral particle (ISVP). When ISVP formation is prevented, reovirus fails to establish a productive infection, suggesting proteolytic priming is required for entry. ISVPs are then converted to ISVP*s, which is accompanied by μ1 rearrangements. The μ1 and σ3 proteins confer resistance to inactivating agents; however, neither the impact on capsid properties nor the mechanism (or basis) of inactivation is fully understood. Here, we utilized T1L/T3D M2 and T3D/T1L S4 to investigate the determinants of reovirus stability. Both reassortants encode mismatched subunits. When μ1-σ3 were derived from different strains, virions resembled wild-type particles in structure and protease sensitivity. T1L/T3D M2 and T3D/T1L S4 ISVPs were less thermostable than wild-type ISVPs. In contrast, virions were equally susceptible to heating. Virion associated μ1 adopted an ISVP*-like conformation concurrent with inactivation; σ3 preserves infectivity by preventing μ1 rearrangements. Moreover, thermostability was enhanced by a hyperstable variant of μ1. Unlike the outer capsid, the inner capsid (core) was highly resistant to elevated temperatures. The dual layered architecture allowed for differential sensitivity to inactivating agents.

Indexed as

AnimalsCapsidCapsid ProteinsCell LineCryoelectron MicroscopyMiceModels, MolecularProtein ConformationProtein StabilityReoviridaeThermodynamicsVirus InternalizationCapsid Proteinscapsid stabilityreassortmentreovirusthree-dimensional structure

Identifiers

PMID30381491
PMCPMC6321938
OpenAlexW2898634673

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.