Evidence map›Paper›PMID 31434934›Full record

ArticleScientific reports2019

Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway.

Florian Sonthonnax, Benoit Besson, Emilie Bonnaud, Grégory Jouvion, David Merino, Florence Larrous, Hervé Bourhy

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

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  9. Regulation of innate immune responses by rabies virus.Animal models and experimental medicine · 2022
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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

7 authors at 3 institutions in 1 country.

Florian SonthonnaxUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
Benoit BessonUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
Emilie BonnaudUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
Grégory JouvionUnité de Neuropathologie expérimentale, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
David MerinoUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
Florence LarrousUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France. florence.larrous@pasteur.fr.
Hervé BourhyUnité Lyssavirus, Epidémiologie et Neuropathologie, Institut Pasteur, 28, rue du Docteur Roux, 75724, Paris, Cedex 15, France.
Institut Pasteur · FRDélégation Paris 7 · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2-TPL2 complex, to efficiently inhibit the nuclear factor-κB (NF-κB) pathway. Using transfections, protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein in the control of Jak-Stat signaling pathway, in synergy with the P protein. In unstimulated cells, both M and P proteins were found to interact with JAK1. Upon type-I IFN stimulation, the M switches toward pSTAT1 interaction, which results in an enhanced capacity of P protein to interact with pSTAT1 and restrain it in the cytoplasm. Furthermore, the role for M-protein positions 77, 100, 104 and 110 was also demonstrated in interaction with both JAK1 and pY-STAT1, and confirmed in vivo. Together, these data indicate that M protein cooperates with P protein to restrain in parallel, and sequentially, NF-κB and Jak-Stat pathways.

Indexed as

Signal TransductionAnimalsCytoplasmHeLa CellsHumansImmunity, InnateInterferon Type IJanus Kinase 1LyssavirusMiceMice, Inbred BALB CMutagenesis, Site-DirectedNF-kappa BPhosphoproteinsPromoter Regions, GeneticSTAT1 Transcription FactorInterferon Type IJAK1 protein, humanJanus Kinase 1NF-kappa BPhosphoproteinsSTAT1 protein, humanSTAT1 Transcription FactorViral Matrix ProteinsViral Proteins

Identifiers

PMID31434934
PMCPMC6704159
OpenAlexW2969296972

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.