Evidence map›Paper›PMID 33082259›Full record

ArticlemBio2020

Inhibition of Coronavirus Entry

Victor K Outlaw, Francesca T Bovier, Megan C Mears, Maria N Cajimat, Yun Zhu, Michelle J Lin, Amin Addetia, Nicole A P Lieberman, Vikas Peddu, Xuping Xie and 6 more

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
1.8field-weighted citation impact, top 8% 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

61 citing papers in PubMed, 83 citations in OpenAlex.

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

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

16 authors at 6 institutions in 3 countries.

Victor K Outlaw *Department of Chemistry, University of Wisconsin, Madison, Wisconsin, USA.ORCID 0000-0001-7054-4204
Francesca T Bovier *Department of Pediatrics, Columbia University Medical Center, New York, New York, USA.
Megan C MearsGalveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA.
Maria N CajimatGalveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA.
Yun ZhuDepartment of Pediatrics, Columbia University Medical Center, New York, New York, USA.
Michelle J LinDepartment of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA.
Amin AddetiaDepartment of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA.
Nicole A P LiebermanDepartment of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA.
Vikas PedduDepartment of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA.
Xuping XieDepartment of Pediatrics, Columbia University Medical Center, New York, New York, USA.ORCID 0000-0003-0918-016X
Pei-Yong ShiDepartment of Pediatrics, Columbia University Medical Center, New York, New York, USA.
Alexander L GreningerDepartment of Laboratory Medicine, University of Washington School of Medicine, Seattle, Washington, USA.ORCID 0000-0002-7443-0527
Samuel H GellmanDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin, USA gellman@chem.wisc.edu dabente@UTMB.EDU am939@cumc.columbia.edu mp3509@cumc.columbia.edu.
Dennis A BenteGalveston National Laboratory, University of Texas Medical Branch, Galveston, Texas, USA gellman@chem.wisc.edu dabente@UTMB.EDU am939@cumc.columbia.edu mp3509@cumc.columbia.edu.
Anne MosconaDepartment of Pediatrics, Columbia University Medical Center, New York, New York, USA gellman@chem.wisc.edu dabente@UTMB.EDU am939@cumc.columbia.edu mp3509@cumc.columbia.edu.
Matteo PorottoDepartment of Pediatrics, Columbia University Medical Center, New York, New York, USA gellman@chem.wisc.edu dabente@UTMB.EDU am939@cumc.columbia.edu mp3509@cumc.columbia.edu.
University of Washington · USColumbia University Irving Medical Center · USThe University of Texas Medical Branch at Galveston · USUniversity of Campania "Luigi Vanvitelli" · ITUniversity of Wisconsin–Madison · USCapital Medical University · CN

Funding

Tumor Biology and Microenvironment ProgramP30CA013696 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI Anil K Rustgi · 1985 to 2026
$115.3M
Protein Recognition by Peptidic FoldamersR01GM056414 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 1997 to 2023
$6.5M
Engineering protease-resistant alpha-beta peptides for broad-spectrum antiviralsR01AI114736 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOSCONA, ANNE · 2015 to 2019
$3.7M
Development of novel endosome-targeted Ebola virus entry inhibitors as antiviral agentsR01AI121349 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI POROTTO, MATTEO · 2016 to 2020
$3.2M
Mechanisms of measles virus CNS adaptationR01NS091263 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI POROTTO, MATTEO · 2015 to 2019
$1.9M
Small molecules to block measles spreading in the central nervous systemR56AI146980 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI POROTTO, MATTEO · 2019 to 2019
$493k
NCI NIH HHS P30 CA013696NIAID NIH HHS R01 AI114736NIAID NIH HHS R01 AI121349NIAID NIH HHS R56 AI146980NIGMS NIH HHS R01 GM056414NINDS NIH HHS R01 NS091263
6 · The paper itself

Abstract

The emergence of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2), the etiological agent of the 2019 coronavirus disease (COVID-19), has erupted into a global pandemic that has led to tens of millions of infections and hundreds of thousands of deaths worldwide. The development of therapeutics to treat infection or as prophylactics to halt viral transmission and spread is urgently needed. SARS-CoV-2 relies on structural rearrangements within a spike (S) glycoprotein to mediate fusion of the viral and host cell membranes. Here, we describe the development of a lipopeptide that is derived from the C-terminal heptad repeat (HRC) domain of SARS-CoV-2 S that potently inhibits infection by SARS-CoV-2. The lipopeptide inhibits cell-cell fusion mediated by SARS-CoV-2 S and blocks infection by live SARS-CoV-2 in Vero E6 cell monolayers more effectively than previously described lipopeptides. The SARS-CoV-2 lipopeptide exhibits broad-spectrum activity by inhibiting cell-cell fusion mediated by SARS-CoV-1 and Middle East respiratory syndrome coronavirus (MERS-CoV) and blocking infection by live MERS-CoV in cell monolayers. We also show that the SARS-CoV-2 HRC-derived lipopeptide potently blocks the spread of SARS-CoV-2 in human airway epithelial (HAE) cultures, an

Indexed as

Amino Acid SequenceAnimalsAntiviral AgentsBetacoronavirusChlorocebus aethiopsCoronavirus InfectionsCOVID-19HEK293 CellsHumansLipopeptidesMembrane FusionMiddle East Respiratory Syndrome CoronavirusPandemicsPneumonia, ViralProtein DomainsRespiratory MucosaAntiviral AgentsLipopeptidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2fusion inhibitorlipopeptideSARS-CoV-2spike protein

Identifiers

PMID33082259
PMCPMC7587434
OpenAlexW3093585860

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.