Evidence map›Paper›PMID 36067270›Full record

ArticlePLoS pathogens2022

Components of the LINC and NPC complexes coordinately target and translocate a virus into the nucleus to promote infection.

Chelsey C Spriggs, Grace Cha, Jiaqian Li, Billy Tsai

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

5 citing papers in PubMed, 7 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

4 authors at 1 institution in 1 country.

Chelsey C SpriggsDepartment of Cell and Developmental Biology, University of Michigan Medical School Ann Arbor, Michigan, United States of America.ORCID 0000-0003-1246-7823
Grace ChaDepartment of Cell and Developmental Biology, University of Michigan Medical School Ann Arbor, Michigan, United States of America.
Jiaqian LiDepartment of Cell and Developmental Biology, University of Michigan Medical School Ann Arbor, Michigan, United States of America.
Billy TsaiDepartment of Cell and Developmental Biology, University of Michigan Medical School Ann Arbor, Michigan, United States of America.
University of Michigan · US

Funding

Transport of polyomavirus across the ER membraneR01AI064296 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TSAI, BILLY · 2006 to 2021
$5.5M
Hijacking host cellular motors for the nuclear entry of polyomavirusesR00GM141365 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SPRIGGS, CHELSEY CIERRA · 2022 to 2024
$747k
Hijacking host cellular motors for the nuclear entry of polyomavirusesK99GM141365 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SPRIGGS, CHELSEY CIERRA · 2021 to 2022
$119k
Clarifying the role of the cytoplasmic dynein motor complex in polyomavirus nuclear entry.F32GM133099 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SPRIGGS, CHELSEY CIERRA · 2019 to 2020
$106k
NIAID NIH HHS R01 AI064296NIGMS NIH HHS F32 GM133099NIGMS NIH HHS K99 GM141365NIGMS NIH HHS R00 GM141365
6 · The paper itself

Abstract

Nuclear entry represents the final and decisive infection step for most DNA viruses, although how this is accomplished by some viruses is unclear. Polyomavirus SV40 transports from the cell surface through the endosome, the endoplasmic reticulum, and the cytosol from where it enters the nucleus to cause infection. Here we elucidate the nuclear entry mechanism of SV40. Our results show that cytosol-localized SV40 is targeted to the nuclear envelope by directly engaging Nesprin-2 of the linker of nucleoskeleton and cytoskeleton (LINC) nuclear membrane complex. Additionally, we identify the NUP188 subunit of the nuclear pore complex (NPC) as a new Nesprin-2-interacting partner. This physical proximity positions the NPC to capture SV40 upon release from Nesprin-2, enabling the channel to facilitate nuclear translocation of the virus. Strikingly, SV40 disassembles during nuclear entry, generating a viral genome-VP1-VP3 subcomplex that efficiently crosses the NPC to enter the nucleus. Our results reveal how two major nuclear membrane protein complexes are exploited to promote targeting and translocation of a virus into the nucleus.

Indexed as

Nuclear PoreVirusesCell NucleusCytoskeletonNuclear EnvelopeNuclear Matrix

Identifiers

PMID36067270
PMCPMC9481172
OpenAlexW4294798316

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.