Evidence map›Paper›PMID 33590968›Full record

ArticleMolecular systems biology2021

SARS-CoV-2 infection remodels the host protein thermal stability landscape.

Joel Selkrig, Megan Stanifer, André Mateus, Karin Mitosch, Inigo Barrio-Hernandez, Mandy Rettel, Heeyoung Kim, Carlos G P Voogdt, Philipp Walch, Carmon Kee and 10 more

Open access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-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

20 citing papers in PubMed, 37 citations in OpenAlex.

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  16. Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021
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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

20 authors at 6 institutions in 2 countries.

Joel SelkrigGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0003-2977-4408
Megan StaniferDepartment of Infectious Diseases, Molecular Virology, Heidelberg University Hospital, Heidelberg, Germany.ORCID 0000-0002-5606-1297
André MateusGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0001-6870-0677
Karin MitoschGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Inigo Barrio-HernandezEuropean Bioinformatics Institute (EMBL-EBI), Hinxton, UK.
Mandy RettelProteomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Heeyoung KimDepartment of Infectious Diseases, Molecular Virology, Heidelberg University Hospital, Heidelberg, Germany.
Carlos G P VoogdtGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Philipp WalchGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Carmon KeeDepartment of Infectious Diseases, Molecular Virology, Heidelberg University Hospital, Heidelberg, Germany.ORCID 0000-0001-5847-5509
Nils KurzawaGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0002-7846-2817
Frank SteinProteomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0001-9695-1692
Clément PotelGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Anna JarzabProteomics and Bioanalytics, Technical University of Munich, Freising, Germany.
Bernhard KusterProteomics and Bioanalytics, Technical University of Munich, Freising, Germany.ORCID 0000-0002-9094-1677
Ralf BartenschlagerDepartment of Infectious Diseases, Molecular Virology, Heidelberg University Hospital, Heidelberg, Germany.ORCID 0000-0001-5601-9307
Steeve BoulantDepartment of Infectious Diseases, Virology, Heidelberg University Hospital, Heidelberg, Germany.ORCID 0000-0001-8614-4993
Pedro BeltraoEuropean Bioinformatics Institute (EMBL-EBI), Hinxton, UK.ORCID 0000-0002-2724-7703
Athanasios TypasGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0002-0797-9018
Mikhail M SavitskiGenome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0003-2011-9247
European Molecular Biology Laboratory · DEHeidelberg University · DEEuropean Bioinformatics Institute · GBEuropean Molecular Biology Organization · DEGerman Cancer Research Center · DETechnical University of Munich · DE

Funding

Bundesministerium für Bildung und Forschung (BMBF) 01KI20198ADeutsche Forschungsgemeinschaft (DFG) 240245660Deutsche Forschungsgemeinschaft (DFG) 272983813Deutsche Forschungsgemeinschaft (DFG) 278001972Deutsche Forschungsgemeinschaft (DFG) 415089553Deutsche Forschungsgemeinschaft (DFG) 416072091EC | H2020 | H2020 Priority Excellent Science | H2020 European Research Council (ERC) 819454German Center for Infection Research (DZIF) 8029705705German Center for Infection Research (DZIF) 8029801806
6 · The paper itself

Abstract

The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a global threat to human health and has compromised economic stability. In addition to the development of an effective vaccine, it is imperative to understand how SARS-CoV-2 hijacks host cellular machineries on a system-wide scale so that potential host-directed therapies can be developed. In situ proteome-wide abundance and thermal stability measurements using thermal proteome profiling (TPP) can inform on global changes in protein activity. Here we adapted TPP to high biosafety conditions amenable to SARS-CoV-2 handling. We discovered pronounced temporal alterations in host protein thermostability during infection, which converged on cellular processes including cell cycle, microtubule and RNA splicing regulation. Pharmacological inhibition of host proteins displaying altered thermal stability or abundance during infection suppressed SARS-CoV-2 replication. Overall, this work serves as a framework for expanding TPP workflows to globally important human pathogens that require high biosafety containment and provides deeper resolution into the molecular changes induced by SARS-CoV-2 infection.

Indexed as

Host-Pathogen InteractionsProtein StabilityAntiviral AgentsCOVID-19HumansProteomeSARS-CoV-2TemperatureViral ProteinsVirus ReplicationAntiviral AgentsProteomeViral Proteinsaryl hydrocarbon hydroxylaseheat shock chaperonerhapontigeninSARS-CoV-2tanespimycin

Identifiers

PMID33590968
PMCPMC7885171
OpenAlexW3112817854

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.