Evidence map›Paper›PMID 27486199›Full record

ArticleMolecular & cellular proteomics : MCP2016

Phosphoproteomics to Characterize Host Response During Influenza A Virus Infection of Human Macrophages.

Sandra Söderholm, Denis E Kainov, Tiina Öhman, Oxana V Denisova, Bert Schepens, Evgeny Kulesskiy, Susumu Y Imanishi, Garry Corthals, Petteri Hintsanen, Tero Aittokallio and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 76 citations in OpenAlex.

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  19. Particulate matter (PMEnvironmental pollution (Barking, Essex : 1987) · 2020
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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

13 authors at 8 institutions in 3 countries.

Sandra SöderholmFrom the ‡Institute of Biotechnology, FI-00014 University of Helsinki, Helsinki, Finland; §Unit of Systems Toxicology, Finnish Institute of Occupational Health, FI-00250 Helsinki, Finland.
Denis E Kainov¶Institute for Molecular Medicine Finland (FIMM), FI-00014 University of Helsinki, Helsinki, Finland.
Tiina ÖhmanFrom the ‡Institute of Biotechnology, FI-00014 University of Helsinki, Helsinki, Finland.
Oxana V Denisova¶Institute for Molecular Medicine Finland (FIMM), FI-00014 University of Helsinki, Helsinki, Finland.
Bert Schepens‖Medical Biotechnology Center, VIB, B-9052 Ghent (Zwijnaarde), Belgium; **Department of Biomedical Molecular Biology, B-9052 Ghent University, Ghent, Belgium.
Evgeny Kulesskiy¶Institute for Molecular Medicine Finland (FIMM), FI-00014 University of Helsinki, Helsinki, Finland.
Susumu Y Imanishi‡‡Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, FI-20520 Turku, Finland.
Garry Corthals‡‡Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, FI-20520 Turku, Finland.
Petteri Hintsanen¶Institute for Molecular Medicine Finland (FIMM), FI-00014 University of Helsinki, Helsinki, Finland.
Tero Aittokallio¶Institute for Molecular Medicine Finland (FIMM), FI-00014 University of Helsinki, Helsinki, Finland.
Xavier Saelens‖Medical Biotechnology Center, VIB, B-9052 Ghent (Zwijnaarde), Belgium; **Department of Biomedical Molecular Biology, B-9052 Ghent University, Ghent, Belgium.
Sampsa Matikainen§§Department of Rheumatology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Tuula A NymanFrom the ‡Institute of Biotechnology, FI-00014 University of Helsinki, Helsinki, Finland; ¶¶Institute of Clinical Medicine, University of Oslo, Norway tuula.nyman@medisin.uio.no.
University of Helsinki · FIInstitute for Molecular Medicine Finland · FIGhent University · BEHelsinki Institute of Physics · FIHelsinki University Hospital · FITurku Centre for Biotechnology · FIUniversity of Turku · FIVIB-UGent Center for Medical Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Influenza A viruses cause infections in the human respiratory tract and give rise to annual seasonal outbreaks, as well as more rarely dreaded pandemics. Influenza A viruses become quickly resistant to the virus-directed antiviral treatments, which are the current main treatment options. A promising alternative approach is to target host cell factors that are exploited by influenza viruses. To this end, we characterized the phosphoproteome of influenza A virus infected primary human macrophages to elucidate the intracellular signaling pathways and critical host factors activated upon influenza infection. We identified 1675 phosphoproteins, 4004 phosphopeptides and 4146 nonredundant phosphosites. The phosphorylation of 1113 proteins (66%) was regulated upon infection, highlighting the importance of such global phosphoproteomic profiling in primary cells. Notably, 285 of the identified phosphorylation sites have not been previously described in publicly available phosphorylation databases, despite many published large-scale phosphoproteome studies using human and mouse cell lines. Systematic bioinformatics analysis of the phosphoproteome data indicated that the phosphorylation of proteins involved in the ubiquitin/proteasome pathway (such as TRIM22 and TRIM25) and antiviral responses (such as MAVS) changed in infected macrophages. Proteins known to play roles in small GTPase-, mitogen-activated protein kinase-, and cyclin-dependent kinase- signaling were also regulated by phosphorylation upon infection. In particular, the influenza infection had a major influence on the phosphorylation profiles of a large number of cyclin-dependent kinase substrates. Functional studies using cyclin-dependent kinase inhibitors showed that the cyclin-dependent kinase activity is required for efficient viral replication and for activation of the host antiviral responses. In addition, we show that cyclin-dependent kinase inhibitors protect IAV-infected mice from death. In conclusion, we provide the first comprehensive phosphoproteome characterization of influenza A virus infection in primary human macrophages, and provide evidence that cyclin-dependent kinases represent potential therapeutic targets for more effective treatment of influenza infections.

Indexed as

AnimalsComputational BiologyCyclin-Dependent KinasesGene Expression RegulationHost-Pathogen InteractionsHumansInfluenza A virusInfluenza, HumanMacrophagesMicePhosphoproteinsProteomicsSignal TransductionCyclin-Dependent KinasesPhosphoproteins

Identifiers

PMID27486199
PMCPMC5054344
OpenAlexW2482044921

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.