Evidence map›Paper›PMID 32779780›Full record

ArticleJournal of computational chemistry2020

Atomistic simulation reveals structural mechanisms underlying D614G spike glycoprotein-enhanced fitness in SARS-COV-2.

I Olaposi Omotuyi, Oyekanmi Nash, O Basiru Ajiboye, C Gift Iwegbulam, E Babatunji Oyinloye, O Abimbola Oyedeji, Z Abimbola Kashim, Kunle Okaiyeto

Abstract read
In one paragraph

Article in Journal of computational chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
–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

31 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  10. Journal of biomolecular structure & dynamics · 2022
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  15. The virological impacts of SARS-CoV-2 D614G mutation.Journal of molecular cell biology · 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

8 authors.

I Olaposi OmotuyiChemo-genomics Research Unit, Department of Biochemistry, Adekunle Ajasin University, Akungba-Akoko, Ondo State, Nigeria.ORCID https://orcid.org/0000-0002-5473-745X
Oyekanmi NashCenter for Genomics Research and Innovation, National Biotechnology Development Agency, Abuja, Nigeria.
O Basiru AjiboyePhytomedicine, Biochemical Toxicology and Biotechnology Research Laboratories, Department of Biochemistry, College of Sciences, Afe Babalola University, Ado-Ekiti, Nigeria.
C Gift IwegbulamCenter for Genomics Research and Innovation, National Biotechnology Development Agency, Abuja, Nigeria.
E Babatunji OyinloyePhytomedicine, Biochemical Toxicology and Biotechnology Research Laboratories, Department of Biochemistry, College of Sciences, Afe Babalola University, Ado-Ekiti, Nigeria.
O Abimbola OyedejiBio-Computing Research Unit, Mols and Sims, Ado-Ekiti, Ekiti State, Nigeria.
Z Abimbola KashimCenter for Genomics Research and Innovation, National Biotechnology Development Agency, Abuja, Nigeria.
Kunle OkaiyetoApplied and Environmental Microbiology Research Group (AEMREG), Department of Biochemistry and Microbiology, University of Fort Hare. Alice campus, Alice, South Africa.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

D614G spike glycoprotein (sgp) mutation in rapidly spreading severe acute respiratory syndrome coronavirus-2 (SARS-COV-2) is associated with enhanced fitness and higher transmissibility in new cases of COVID-19 but the underlying mechanism is unknown. Here, using atomistic simulation, a plausible mechanism has been delineated. In G614 sgp but not wild type, increased D(G)614-T859 Cα-distance within 65 ns is interpreted as S1/S2 protomer dissociation. Overall, ACE2-binding, post-fusion core, open-state and sub-optimal antibody-binding conformations were preferentially sampled by the G614 mutant, but not wild type. Furthermore, in the wild type, only one of the three sgp chains has optimal communication route between residue 614 and the receptor-binding domain (RBD); whereas, two of the three chains communicated directly in G614 mutant. These data provide evidence that D614G sgp mutant is more available for receptor binding, cellular invasion and reduced antibody interaction; thus, providing framework for enhanced fitness and higher transmissibility in D614G SARS-COV-2 mutant.

Indexed as

Computer SimulationModels, ChemicalAmino Acid SequenceBetacoronavirusBinding SitesCoronavirus InfectionsCOVID-19HumansModels, MolecularMutationPandemicsPneumonia, ViralProtein BindingProtein ConformationProtein DomainsSARS-CoV-2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID‐19molecular dynamics simulationmutationSARS‐COV‐2spike glycoprotein

Identifiers

PMID32779780
PMCPMC7404873

What OpenQuestion holds

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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.