Evidence map›Paper›PMID 29632367›Full record

ArticleNature microbiology2018

Proteotype profiling unmasks a viral signalling network essential for poxvirus assembly and transcriptional competence.

Karel Novy, Samuel Kilcher, Ulrich Omasits, Christopher Karl Ernst Bleck, Corina Beerli, Jakob Vowinckel, Caroline K Martin, Mohammedyaseen Syedbasha, Alessio Maiolica, Ian White and 2 more

Abstract read
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In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 4 institutions in 2 countries.

Karel NovyInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Samuel KilcherMRC-Laboratory for Molecular Cell Biology, University College London, London, UK.ORCID 0000-0002-1162-6549
Ulrich OmasitsInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Christopher Karl Ernst BleckCenter for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Basel, Switzerland.
Corina BeerliMRC-Laboratory for Molecular Cell Biology, University College London, London, UK.
Jakob VowinckelBiognosys AG, Schlieren, Switzerland.ORCID 0000-0002-4343-4058
Caroline K MartinMRC-Laboratory for Molecular Cell Biology, University College London, London, UK.
Mohammedyaseen SyedbashaInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Alessio MaiolicaInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland.
Ian WhiteMRC-Laboratory for Molecular Cell Biology, University College London, London, UK.
Jason MercerMRC-Laboratory for Molecular Cell Biology, University College London, London, UK. jason.mercer@ucl.ac.uk.ORCID 0000-0003-1466-9541
Bernd WollscheidInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Zurich, Switzerland. wbernd@ethz.ch.ORCID 0000-0002-3923-1610
ETH Zurich · CHMRC Laboratory for Molecular Cell Biology · GBBiognosys (Switzerland) · CHUniversity of Basel · CH

Funding

Electron Microscopy CoreZICHL005906 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SYED, ZULFEQHAR · 2009 to 2025
$12.9M
Medical Research Council MC_UU_12018/7
6 · The paper itself

Abstract

To orchestrate context-dependent signalling programmes, poxviruses encode two dual-specificity enzymes, the F10 kinase and the H1 phosphatase. These signalling mediators are essential for poxvirus production, yet their substrate profiles and systems-level functions remain enigmatic. Using a phosphoproteomic screen of cells infected with wild-type, F10 and H1 mutant vaccinia viruses, we systematically defined the viral signalling network controlled by these enzymes. Quantitative cross-comparison revealed 33 F10 and/or H1 phosphosites within 17 viral proteins. Using this proteotype dataset to inform genotype-phenotype relationships, we found that H1-deficient virions harbour a hidden hypercleavage phenotype driven by reversible phosphorylation of the virus protease I7 (S134). Quantitative phosphoproteomic profiling further revealed that the phosphorylation-dependent activity of the viral early transcription factor, A7 (Y367), underlies the transcription-deficient phenotype of H1 mutant virions. Together, these results highlight the utility of combining quantitative proteotype screens with mutant viruses to uncover proteotype-phenotype-genotype relationships that are masked by classical genetic studies.

Indexed as

MutationGene Expression Regulation, ViralGene Regulatory NetworksHeLa CellsHumansPhenotypePhosphoproteinsPhosphoric Monoester HydrolasesProtein Serine-Threonine KinasesProteomicsSignal TransductionVaccinia virusViral ProteinsVirus AssemblyPhosphoproteinsPhosphoric Monoester Hydrolasesprotein kinase 2, Vaccinia virusProtein Serine-Threonine KinasesViral Proteins

Identifiers

PMID29632367
OpenAlexW2559833114

What OpenQuestion holds

Textmetadata
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.