Evidence map›Paper›PMID 36216808›Full record

ArticleNature communications2022

Membrane-assisted assembly and selective secretory autophagy of enteroviruses.

Selma Dahmane, Adeline Kerviel, Dustin R Morado, Kasturika Shankar, Björn Ahlman, Michael Lazarou, Nihal Altan-Bonnet, Lars-Anders Carlson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
7.1field-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

33 citing papers in PubMed, 47 citations in OpenAlex.

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  17. Nonlytic Egress and Transmission in the Virus World.Annual review of biochemistry · 2025
    Review
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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

8 authors at 4 institutions in 3 countries.

Selma DahmaneDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Adeline KervielLaboratory of Host-Pathogen Dynamics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Dustin R MoradoDepartment of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Stockholm, Sweden.ORCID 0000-0003-4693-3220
Kasturika ShankarDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Björn AhlmanDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden.
Michael LazarouDepartment of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Melbourne, Australia.ORCID 0000-0003-2150-5545
Nihal Altan-BonnetLaboratory of Host-Pathogen Dynamics, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-5546-6452
Lars-Anders CarlsonDepartment of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden. lars-anders.carlson@umu.se.ORCID 0000-0003-2342-6488
Umeå University · SENational Institutes of Health · USAustralian Regenerative Medicine Institute · AUStockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enteroviruses are non-enveloped positive-sense RNA viruses that cause diverse diseases in humans. Their rapid multiplication depends on remodeling of cytoplasmic membranes for viral genome replication. It is unknown how virions assemble around these newly synthesized genomes and how they are then loaded into autophagic membranes for release through secretory autophagy. Here, we use cryo-electron tomography of infected cells to show that poliovirus assembles directly on replication membranes. Pharmacological untethering of capsids from membranes abrogates RNA encapsidation. Our data directly visualize a membrane-bound half-capsid as a prominent virion assembly intermediate. Assembly progression past this intermediate depends on the class III phosphatidylinositol 3-kinase VPS34, a key host-cell autophagy factor. On the other hand, the canonical autophagy initiator ULK1 is shown to restrict virion production since its inhibition leads to increased accumulation of virions in vast intracellular arrays, followed by an increased vesicular release at later time points. Finally, we identify multiple layers of selectivity in virus-induced autophagy, with a strong selection for RNA-loaded virions over empty capsids and the segregation of virions from other types of autophagosome contents. These findings provide an integrated structural framework for multiple stages of the poliovirus life cycle.

Indexed as

Enterovirus InfectionsPoliovirusAutophagyCapsidClass III Phosphatidylinositol 3-KinasesHumansRNAVirionVirus AssemblyClass III Phosphatidylinositol 3-KinasesRNA

Identifiers

PMID36216808
PMCPMC9550805
OpenAlexW4304098669

What Socratic 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 Socratic graph.