Evidence map›Paper›PMID 35019723›Full record

ArticleJournal of virology2022

Rapid SARS-CoV-2 Adaptation to Available Cellular Proteases.

M Zeeshan Chaudhry, Kathrin Eschke, Markus Hoffmann, Martina Grashoff, Leila Abassi, Yeonsu Kim, Linda Brunotte, Stephan Ludwig, Andrea Kröger, Frank Klawonn and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 38 citations in OpenAlex.

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  7. AnmBio · 2024
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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

12 authors at 4 institutions in 1 country.

M Zeeshan Chaudhry *Department of Viral Immunology, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.ORCID 0000-0002-1372-4257
Kathrin Eschke *Department of Viral Immunology, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Markus HoffmannInfection Biology Unit, German Primate Centergrid.418215.b, Göttingen, Germany.
Martina GrashoffResearch Group Innate Immunity and Infection, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Leila AbassiDepartment of Viral Immunology, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Yeonsu KimDepartment of Viral Immunology, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Linda BrunotteInstitut für Virologie (IMV), Westfälische Wilhelms-Universität Münster, Münster, Germany.
Stephan LudwigInstitut für Virologie (IMV), Westfälische Wilhelms-Universität Münster, Münster, Germany.ORCID 0000-0003-4490-3052
Andrea KrögerResearch Group Innate Immunity and Infection, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Frank KlawonnBiostatistics Group, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.
Stefan H PöhlmannInfection Biology Unit, German Primate Centergrid.418215.b, Göttingen, Germany.ORCID 0000-0001-6086-9136
Luka Cicin-SainDepartment of Viral Immunology, Helmholtz Centre for Infection Researchgrid.7490.a, Braunschweig, Germany.ORCID 0000-0003-3978-778X
Helmholtz Centre for Infection Research · DEGerman Primate Center · DEUniversity of Münster · DEOstfalia University of Applied Sciences · DE

Funding

Helmholtz Association () PIE-0008
6 · The paper itself

Abstract

Recent emergence of SARS-CoV-1 variants demonstrates the potential of this virus for targeted evolution, despite its overall genomic stability. Here we show the dynamics and the mechanisms behind the rapid adaptation of SARS-CoV-2 to growth in Vero E6 cells. The selective advantage for growth in Vero E6 cells is due to increased cleavage efficiency by cathepsins at the mutated S1/S2 site. S1/S2 site also constitutes a heparan sulfate (HS) binding motif that influenced virus growth in Vero E6 cells, but HS antagonist did not inhibit virus adaptation in these cells. The entry of Vero E6-adapted virus into human cells is defective because the mutated spike variants are poorly processed by furin or TMPRSS2. Minor subpopulation that lack the furin cleavage motif in the spike protein rapidly become dominant upon passaging through Vero E6 cells, but wild type sequences are maintained at low percentage in the virus swarm and mediate a rapid reverse adaptation if the virus is passaged again on TMPRSS2

Indexed as

Adaptation, PhysiologicalAnimalsChlorocebus aethiopsCOVID-19Cytopathogenic Effect, ViralFurinHEK293 CellsHigh-Throughput Nucleotide SequencingHumansMutationSARS-CoV-2Serine EndopeptidasesSpike Glycoprotein, CoronavirusVero CellsVirus ReplicationFurinSerine EndopeptidasesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2coronavirus spike primingdeep sequencingfurin cleavage siteSARS-CoV-2spike mutation

Identifiers

PMID35019723
PMCPMC8906416
OpenAlexW4221019220

What OpenQuestion holds

Textmetadata
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.