Evidence map›Paper›PMID 32941612›Full record

ArticleMolecular biology and evolution2021

Potential Pathogenicity Determinants Identified from Structural Proteomics of SARS-CoV and SARS-CoV-2.

Erica T Prates, Michael R Garvin, Mirko Pavicic, Piet Jones, Manesh Shah, Omar Demerdash, B Kirtley Amos, Armin Geiger, Daniel Jacobson

Open access · hybridAbstract read
In one paragraph

Article in Molecular biology and evolution, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  6. The origins of COVID-19 pandemic: A brief overview.Transboundary and emerging diseases · 2022
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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

9 authors at 4 institutions in 1 country.

Erica T PratesBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN.
Michael R GarvinBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN.
Mirko PavicicBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN.
Piet JonesNational Virtual Biotechnology Laboratory, US Department of Energy, TN.
Manesh ShahGenome Science and Technology, The University of Tennessee Knoxville, Knoxville, TN.
Omar DemerdashBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN.
B Kirtley AmosDepartment of Horticulture, N-318 Ag Sciences Center, University of Kentucky, Lexington, KY.
Armin GeigerNational Virtual Biotechnology Laboratory, US Department of Energy, TN.
Daniel JacobsonBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN.
Oak Ridge National Laboratory · USNational Energy Technology Laboratory · USUniversity of Kentucky · USUniversity of Tennessee at Knoxville · US

Funding

US Department of Energy DE-AC05-00OR22725
6 · The paper itself

Abstract

Despite SARS-CoV and SARS-CoV-2 being equipped with highly similar protein arsenals, the corresponding zoonoses have spread among humans at extremely different rates. The specific characteristics of these viruses that led to such distinct outcomes remain unclear. Here, we apply proteome-wide comparative structural analysis aiming to identify the unique molecular elements in the SARS-CoV-2 proteome that may explain the differing consequences. By combining protein modeling and molecular dynamics simulations, we suggest nonconservative substitutions in functional regions of the spike glycoprotein (S), nsp1, and nsp3 that are contributing to differences in virulence. Particularly, we explain why the substitutions at the receptor-binding domain of S affect the structure-dynamics behavior in complexes with putative host receptors. Conservation of functional protein regions within the two taxa is also noteworthy. We suggest that the highly conserved main protease, nsp5, of SARS-CoV and SARS-CoV-2 is part of their mechanism of circumventing the host interferon antiviral response. Overall, most substitutions occur on the protein surfaces and may be modulating their antigenic properties and interactions with other macromolecules. Our results imply that the striking difference in the pervasiveness of SARS-CoV-2 and SARS-CoV among humans seems to significantly derive from molecular features that modulate the efficiency of viral particles in entering the host cells and blocking the host immune response.

Indexed as

Molecular Dynamics SimulationProteomicsAnimalsHumansProtein DomainsSARS-CoV-2Severe acute respiratory syndrome-related coronavirusSpecies SpecificityViral ProteinsViral ProteinsCOVID-19pathogenesisproteome-wide analysisproteome-wide modelingSARS-CoVSARS-CoV-2

Identifiers

PMID32941612
PMCPMC7543629
OpenAlexW3087239253

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.