Evidence map›Paper›PMID 32083638›Full record

ArticleThe Biochemical journal2020

Processing of the SARS-CoV pp1a/ab nsp7-10 region.

Boris Krichel, Sven Falke, Rolf Hilgenfeld, Lars Redecke, Charlotte Uetrecht

Abstract read
In one paragraph

Article in The Biochemical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
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

72 citing papers in PubMed.

  1. Article
  2. Review
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  4. MarinePharmaceuticals (Basel, Switzerland) · 2026
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  15. Expression and immunogenicity of non-structural protein 8 of porcine epidemic diarrhea virus.Veterinary research forum : an international quarterly journal · 2024
    Article
  16. Article
  17. Article
  18. Review
  19. Mutations in SARS-CoV-2: Insights on structure, variants, vaccines, and biomedical interventions.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2023
    Review
  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Boris KrichelHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistraße 52, 20251 Hamburg, Germany.
Sven FalkeUniversity of Hamburg, Institut für Biochemie und Molekularbiologie, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
Rolf HilgenfeldUniversity of Lübeck, Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Lars RedeckeUniversity of Lübeck, Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, Ratzeburger Allee 160, 23562 Lübeck, Germany.
Charlotte UetrechtHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistraße 52, 20251 Hamburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus is the causative agent of a respiratory disease with a high case fatality rate. During the formation of the coronaviral replication/transcription complex, essential steps include processing of the conserved polyprotein nsp7-10 region by the main protease Mpro and subsequent complex formation of the released nsp's. Here, we analyzed processing of the coronavirus nsp7-10 region using native mass spectrometry showing consumption of substrate, rise and fall of intermediate products and complexation. Importantly, there is a clear order of cleavage efficiencies, which is influenced by the polyprotein tertiary structure. Furthermore, the predominant product is an nsp7+8(2 : 2) hetero-tetramer with nsp8 scaffold. In conclusion, native MS, opposed to other methods, can expose the processing dynamics of viral polyproteins and the landscape of protein interactions in one set of experiments. Thereby, new insights into protein interactions, essential for generation of viral progeny, were provided, with relevance for development of antivirals.

Indexed as

Coronavirus 3C ProteasesCoronavirus InfectionsCoronavirus RNA-Dependent RNA PolymeraseCysteine EndopeptidasesFluorescence Resonance Energy TransferProtein Structure, SecondaryRNA-Binding ProteinsSequence AlignmentViral Nonstructural ProteinsViral Regulatory and Accessory ProteinsVirus ReplicationCoronavirus 3C ProteasesCoronavirus RNA-Dependent RNA PolymeraseCysteine EndopeptidasesNS8 protein, SARS-CoV-2ORF1ab polyprotein, SARS-CoV-2RNA-Binding ProteinsViral Nonstructural ProteinsViral Regulatory and Accessory Proteinscoronavirusnative mass spectrometrypolyprotein processingstructural virology

Identifiers

PMID32083638
PMCPMC7078746

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Registered trials

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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.