Evidence map›Paper›PMID 32637944›Full record

ArticlebioRxiv : the preprint server for biology2020

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

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

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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

1 citing paper in PubMed, 89 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

22 authors at 4 institutions in 3 countries.

Leonid YurkovetskiyProgram in Molecular Medicine, University of Massachusetts Medical School, 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.
Christopher Tomkins-TinchBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA.
Thomas NyalileProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Yetao WangProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Alina BaumRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591.
William E DiehlProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Ann DauphinProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Claudia CarboneProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Kristen VeinotteProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Shawn B EgriProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Stephen F SchaffnerBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA.
Jacob E LemieuxBroad Institute of Harvard and MIT, 75 Ames Street, Cambridge, MA 02142, USA.
James MunroD epartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Ashique RafiqueRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591.
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.
Christos A KyratsousRegeneron Pharmaceutical, Inc., 777 Old Saw Mill River Rd, Tarrytown, NY 10591.
Natalya DudkinaThermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
Kuang ShenProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Jeremy LubanProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
University of Massachusetts Chan Medical School · USBroad Institute · USRegeneron (United States) · USThermo Fisher Scientific (Netherlands) · NL

Funding

Viral Genomics: evolution, spread, and host interactionsU19AI110818 · NIAID · BROAD INSTITUTE, INC. · PI EARL, ASHLEE MIRIAM · 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
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 AI110818
6 · The paper itself

Abstract

The SARS-CoV-2 spike (S) protein variant D614G supplanted the ancestral virus worldwide in a matter of months. Here we show that D614G was more infectious than the ancestral form on human lung cells, colon cells, and cells rendered permissive by ectopic expression of various mammalian ACE2 orthologs. Nonetheless, 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 a critical interprotomer contact and that this dramatically shifts the S protein trimer conformation toward an ACE2-binding and fusion-competent state. Consistent with the more open conformation, neutralization potency of antibodies targeting the S protein receptor-binding domain was not attenuated. These results indicate that D614G adopts conformations that make virion membrane fusion with the target cell membrane more probable but that D614G retains susceptibility to therapies that disrupt interaction of the SARS-CoV-2 S protein with the ACE2 receptor.

Identifiers

PMID32637944
PMCPMC7337374
OpenAlexW3099115663

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.