Evidence map›Paper›PMID 24823948›Full record

ArticlePloS one2014

ANP32B is a nuclear target of henipavirus M proteins.

Anja Bauer, Sebastian Neumann, Axel Karger, Ann-Kristin Henning, Andrea Maisner, Boris Lamp, Erik Dietzel, Linda Kwasnitschka, Anne Balkema-Buschmann, Günther M Keil and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

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  19. Cracking the ANP32 whips: important functions, unequal requirement, and hints at disease implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014
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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

11 authors at 2 institutions in 1 country.

Anja BauerFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Sebastian NeumannFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Axel KargerFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Ann-Kristin HenningFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Andrea MaisnerInstitute of Virology, Philipps-University Marburg, Marburg, Germany.
Boris LampInstitute of Virology, Philipps-University Marburg, Marburg, Germany.
Erik DietzelInstitute of Virology, Philipps-University Marburg, Marburg, Germany.
Linda KwasnitschkaFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
Anne Balkema-BuschmannFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Novel and Emerging Infectious Diseases, Greifswald - Insel Riems, Germany.
Günther M KeilFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Stefan FinkeFriedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Institute of Molecular Biology, Greifswald - Insel Riems, Germany.
Friedrich-Loeffler-Institut · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane envelopment and budding of negative strand RNA viruses (NSVs) is mainly driven by viral matrix proteins (M). In addition, several M proteins are also known to be involved in host cell manipulation. Knowledge about the cellular targets and detailed molecular mechanisms, however, is poor for many M proteins. For instance, Nipah Virus (NiV) M protein trafficking through the nucleus is essential for virus release, but nuclear targets of NiV M remain unknown. To identify cellular interactors of henipavirus M proteins, tagged Hendra Virus (HeV) M proteins were expressed and M-containing protein complexes were isolated and analysed. Presence of acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) in the complex suggested that this protein represents a direct or indirect interactor of the viral matrix protein. Over-expression of ANP32B led to specific nuclear accumulation of HeV M, providing a functional link between ANP32B and M protein. ANP32B-dependent nuclear accumulation was observed after plasmid-driven expression of HeV and NiV matrix proteins and also in NiV infected cells. The latter indicated that an interaction of henipavirus M protein with ANP32B also occurs in the context of virus replication. From these data we conclude that ANP32B is a nuclear target of henipavirus M that may contribute to virus replication. Potential effects of ANP32B on HeV nuclear shuttling and host cell manipulation by HeV M affecting ANP32B functions in host cell survival and gene expression regulation are discussed.

Indexed as

Cell NucleusFluorescent Antibody Technique, IndirectHEK293 CellsHendra VirusHumansMicroscopy, ConfocalMultiprotein ComplexesNuclear ProteinsTransfectionViral Matrix ProteinsANP32B protein, humanMultiprotein ComplexesNuclear ProteinsViral Matrix Proteins

Identifiers

PMID24823948
PMCPMC4019565
OpenAlexW2047182511

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.