Evidence map›Paper›PMID 36427566›Full record

ArticleJournal of molecular biology2023

Human 14-3-3 Proteins Site-selectively Bind the Mutational Hotspot Region of SARS-CoV-2 Nucleoprotein Modulating its Phosphoregulation.

Kristina V Tugaeva, Andrey A Sysoev, Anna A Kapitonova, Jake L R Smith, Phillip Zhu, Richard B Cooley, Alfred A Antson, Nikolai N Sluchanko

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 31 citations in OpenAlex.

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  5. Evolution of a fuzzy ribonucleoprotein complex in viral assembly.bioRxiv : the preprint server for biology · 2025
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  8. Identification ofMolecules (Basel, Switzerland) · 2025
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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

8 authors at 3 institutions in 3 countries.

Kristina V TugaevaA.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
Andrey A SysoevA.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
Anna A KapitonovaA.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
Jake L R SmithYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom.
Phillip ZhuDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.
Richard B CooleyDepartment of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.
Alfred A AntsonYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, United Kingdom.
Nikolai N SluchankoA.N. Bach Institute of Biochemistry, Federal Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia. Electronic address: nikolai.sluchanko@mail.ru.
A N Bach Institute of Biochemistry · RUOregon State University · USUniversity of York · GB

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
NIGMS NIH HHS RM1 GM144227Wellcome Trust 206377Wellcome Trust 206377/Z/17/Z
6 · The paper itself

Abstract

Phosphorylation of SARS-CoV-2 nucleoprotein recruits human cytosolic 14-3-3 proteins playing a well-recognized role in replication of many viruses. Here we use genetic code expansion to demonstrate that 14-3-3 binding is triggered by phosphorylation of SARS-CoV-2 nucleoprotein at either of two pseudo-repeats centered at Ser197 and Thr205. According to fluorescence anisotropy measurements, the pT205-motif,presentin SARS-CoV-2 but not in SARS-CoV, is preferred over the pS197-motif by all seven human 14-3-3 isoforms, which collectively display an unforeseen pT205/pS197 peptide binding selectivity hierarchy. Crystal structures demonstrate that pS197 and pT205 are mutually exclusive 14-3-3-binding sites, whereas SAXS and biochemical data obtained on the full protein-protein complex indicate that 14-3-3 binding occludes the Ser/Arg-rich region of the nucleoprotein, inhibiting its dephosphorylation. This Ser/Arg-rich region is highly prone to mutations, as exemplified by the Omicron and Delta variants, with our data suggesting that the strength of 14-3-3/nucleoprotein interaction can be linked with the replicative fitness of the virus.

Indexed as

14-3-3 ProteinsCoronavirus Nucleocapsid ProteinsCOVID-19NucleoproteinsSARS-CoV-2HumansMutationPhosphoproteinsScattering, Small AngleX-Ray Diffraction14-3-3 ProteinsCoronavirus Nucleocapsid Proteinsnucleocapsid phosphoprotein, SARS-CoV-2NucleoproteinsPhosphoproteins14-3-3 proteinbinding selectivityhost-virus interactionsphosphopeptide bindingRNA viruses

Identifiers

PMID36427566
PMCPMC9683861
OpenAlexW4309930092

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.