Evidence map›Paper›PMID 36996819›Full record

ArticleCell host & microbe2023

Characterization of the rotavirus assembly pathway in situ using cryoelectron tomography.

Pranav N M Shah, James B Gilchrist, Björn O Forsberg, Alister Burt, Andrew Howe, Shyamal Mosalaganti, William Wan, Julika Radecke, Yuriy Chaban, Geoff Sutton and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Cell host & microbe, 2023. 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
8.0field-weighted citation impact, top 2% 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, 41 citations in OpenAlex.

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  20. Integrative Approaches to Study Virus Structures.Sub-cellular biochemistry · 2024
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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

12 authors at 5 institutions in 3 countries.

Pranav N M ShahDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK; CAMS Oxford Institute, Nuffield Department of Medicine, University of Oxford, Old Road Campus, Headington, Oxford, UK. Electronic address: pranav.shah@strubi.ox.ac.uk.
James B GilchristDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Björn O ForsbergDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK; Department of Physiology and Pharmacology, Karolinska Institute, Stockholm, Sweden.
Alister BurtLaboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, UK.
Andrew HoweDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Shyamal MosalagantiLife Sciences Institute and Department of Cell and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
William WanVanderbilt University Center for Structural Biology, PMB 407917, 465 21st Ave S, 5140 MRB3, Nashville, TN, USA.
Julika RadeckeDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Yuriy ChabanDiamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK.
Geoff SuttonDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK.
David I StuartDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK; CAMS Oxford Institute, Nuffield Department of Medicine, University of Oxford, Old Road Campus, Headington, Oxford, UK; Diamond Light Source Ltd, Harwell Science & Innovation Campus, Didcot, UK. Electronic address: david.stuart@strubi.ox.ac.uk.
Mark BoyceDivision of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford, UK. Electronic address: mark.boyce@strubi.ox.ac.uk.
Centre for Human Genetics · GBDiamond Light Source · GBMRC Laboratory of Molecular Biology · GBUniversity of Michigan · USVanderbilt University · US

Funding

Medical Research Council MR/N00065X/1Wellcome Trust 093305Wellcome Trust 203141
6 · The paper itself

Abstract

Rotavirus assembly is a complex process that involves the stepwise acquisition of protein layers in distinct intracellular locations to form the fully assembled particle. Understanding and visualization of the assembly process has been hampered by the inaccessibility of unstable intermediates. We characterize the assembly pathway of group A rotaviruses observed in situ within cryo-preserved infected cells through the use of cryoelectron tomography of cellular lamellae. Our findings demonstrate that the viral polymerase VP1 recruits viral genomes during particle assembly, as revealed by infecting with a conditionally lethal mutant. Additionally, pharmacological inhibition to arrest the transiently enveloped stage uncovered a unique conformation of the VP4 spike. Subtomogram averaging provided atomic models of four intermediate states, including a pre-packaging single-layered intermediate, the double-layered particle, the transiently enveloped double-layered particle, and the fully assembled triple-layered virus particle. In summary, these complementary approaches enable us to elucidate the discrete steps involved in forming an intracellular rotavirus particle.

Indexed as

RotavirusTomographyVirus Assemblycellular structural biologycryoelectron tomographydsRNA viruseselectron microscopyin situReoviridaerotavirussubtomogram averagingvirus assemblyvirus structure

Identifiers

PMID36996819
PMCPMC7615348
OpenAlexW4361200024

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.