Evidence map›Paper›PMID 33863729›Full record

ArticleScience advances2021

The SARS-CoV-2 Spike variant D614G favors an open conformational state.

Rachael A Mansbach, Srirupa Chakraborty, Kien Nguyen, David C Montefiori, Bette Korber, S Gnanakaran

Abstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
141citing 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

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

  1. Pooled it
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  3. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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81 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Rachael A MansbachTheoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-6738-1261
Srirupa ChakrabortyTheoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-7155-2764
Kien NguyenTheoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0003-0038-5601
David C MontefioriDepartment of Surgery, Duke Human Vaccine Institute, Durham, NC 27710, USA.ORCID 0000-0003-0856-6319
Bette KorberTheoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-2026-5757
S GnanakaranTheoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. gnana@lanl.gov.ORCID 0000-0002-9368-3044

Funding

UNM TRAININGP50GM085273 · NIGMS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI LIDKE, KEITH A · 2009 to 2018
$26.1M
Optimizing glycan shield coverage, germline B cell receptor binding and epitope diversity of V2-apex targeted HIV-1 Env immunogensR37AI150590 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI Beatrice H Hahn · 2019 to 2026
$6.9M
NIAID NIH HHS R37 AI150590NIGMS NIH HHS P50 GM085273
6 · The paper itself

Abstract

The COVID-19 (coronavirus disease 2019) pandemic underwent a rapid transition with the emergence of a dominant viral variant (from the "D-form" to the "G-form") that carried an amino acid substitution D614G in its "Spike" protein. The G-form is more infectious in vitro and is associated with increased viral loads in the upper airways. To gain insight into the molecular-level underpinnings of these characteristics, we used microsecond all-atom simulations. We show that changes in the protein energetics favor a higher population of infection-capable states in the G-form through release of asymmetry present in the D-form inter-protomer interactions. Thus, the increased infectivity of the G-form is likely due to a higher rate of profitable binding encounters with the host receptor. It is also predicted to be more neutralization sensitive owing to enhanced exposure of the receptor binding domain, a key target region for neutralizing antibodies. These results are critical for vaccine design.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme 2Antibodies, NeutralizingCOVID-19GlycosylationHumansHydrogen BondingMolecular Dynamics SimulationMutationProtein BindingProtein Structure, QuaternaryProtein SubunitsSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, NeutralizingProtein SubunitsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID33863729
PMCPMC8051874

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LicenceCC BY-NC
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.