Evidence map›Paper›PMID 32991842›Full record

ArticleCell2020

Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.

Leonid Yurkovetskiy, Xue Wang, Kristen E Pascal, Christopher Tomkins-Tinch, Thomas P Nyalile, Yetao Wang, Alina Baum, William E Diehl, Ann Dauphin, Claudia Carbone and 12 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 704 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
704citing papers in PubMed, 2 pooled it
24.9field-weighted citation impact, top 1% 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

704 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,115 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  11. D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Article
  13. Machine learning-guided rational engineering of ACE2-derived peptides for broad-spectrum neutralization of SARS-CoV-2 variants.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026
    Article
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  18. Glycosylation of GETV E2 promotes pathogenesis in animal models.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

22 authors at 6 institutions in 2 countries.

Leonid YurkovetskiyProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Xue WangThermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
Kristen E PascalRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591, USA.
Christopher Tomkins-TinchBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA; Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA.
Thomas P NyalileProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Yetao WangProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Alina BaumRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591, USA.
William E DiehlProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Ann DauphinProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Claudia CarboneProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Kristen VeinotteProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Shawn B EgriProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Stephen F SchaffnerBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA; Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA.
Jacob E LemieuxBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA; Massachusetts General Hospital, 55 Fruit Street, Boston, MA, 02114, USA.
James B MunroDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, 55 Lake Avenue, Worcester, MA 01605, USA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St, Worcester, MA 01605, USA.
Ashique RafiqueRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591, USA.
Abhi BarveThermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
Pardis C SabetiBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA; Harvard University, 52 Oxford Street, Cambridge, MA 02138, USA; Harvard T.H. Chan School of Public Health, 677 Huntington Avenue, 02115 Boston, MA, USA; Howard Hughes Medical Institute, 4000 Jones Bridge Rd, Chevy Chase, MD 20815, USA; Massachusetts Consortium on Pathogen Readiness, Boston, MA, 02115, USA. Electronic address: pardis.sabeti@broadinstitute.org.
Christos A KyratsousRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591, USA. Electronic address: christos.kyratsous@regeneron.com.
Natalya V DudkinaThermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands. Electronic address: natalya.dudkina@thermofisher.com.
Kuang ShenProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA. Electronic address: kuang.shen@umassmed.edu.
Jeremy LubanProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA; Broad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA; Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St, Worcester, MA 01605, USA; Massachusetts Consortium on Pathogen Readiness, Boston, MA, 02115, USA. Electronic address: jeremy.luban@umassmed.edu.
University of Massachusetts Chan Medical School · USRegeneron (United States) · USThermo Fisher Scientific (Netherlands) · NLConcord Consortium · USHarvard University Press · USMassachusetts General Hospital · US

Funding

Viral Genomics: evolution, spread, and host interactionsU19AI110818 · NIAID · BROAD INSTITUTE, INC. · PI CUOMO, CHRISTINA A · 2014 to 2024
$66.5M
The HUSH complex in HIV-1 latencyR37AI147868 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JEREMY LUBAN · 2019 to 2026
$6.4M
Insight into the Ebola virus glycoprotein fusion mechanism gleaned from the 2013-2016 epidemic GP-A82V variantR01AI148784 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LUBAN, JEREMY · 2020 to 2024
$4.1M
Structural dynamics of single Ebolavirus GP molecules.DP2AI124384 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MUNRO, JAMES B · 2015 to 2015
$2.5M
Spatial and temporal regulation of nutrient sensingR35GM146824 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Kuang Shen · 2022 to 2026
$2.2M
A Molecular Study of Rag GTPase-Dependent Amino Acid SensingK22CA241362 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SHEN, KUANG · 2020 to 2022
$612k
NCI NIH HHS K22 CA241362NIAID NIH HHS DP2 AI124384NIAID NIH HHS R01 AI148784NIAID NIH HHS R37 AI147868NIAID NIH HHS U19 AI110818NIGMS NIH HHS R35 GM146824
6 · The paper itself

Abstract

The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide, reaching near fixation in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin. D614G did not alter S protein synthesis, processing, or incorporation into SARS-CoV-2 particles, but D614G affinity for ACE2 was reduced due to a faster dissociation rate. Assessment of the S protein trimer by cryo-electron microscopy showed that D614G disrupts an interprotomer contact and that the conformation is shifted toward an ACE2 binding-competent state, which is modeled to be on pathway for virion membrane fusion with target cells. Consistent with this more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated.

Indexed as

Angiotensin-Converting Enzyme 2AnimalsAntibodies, MonoclonalAntibodies, ViralBetacoronavirusCells, CulturedCoronavirus InfectionsCOVID-19FemaleGenetic VariationHEK293 CellsHumansMaleModels, MolecularPandemicsPeptidyl-Dipeptidase AACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, ViralPeptidyl-Dipeptidase AReceptors, CoronavirusReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2coronavirusCOVID-19cryo-electron microscopyinfectivityneutralizing antibodypandemicSARS-CoV-2Spike protein

Identifiers

PMID32991842
PMCPMC7492024
OpenAlexW3084653951

What OpenQuestion holds

Textmetadata
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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.