Evidence map›Paper›PMID 34406867›Full record

ArticleJournal of virology2021

Natural and Recombinant SARS-CoV-2 Isolates Rapidly Evolve

Nikita Shiliaev, Tetyana Lukash, Oksana Palchevska, David K Crossman, Todd J Green, Michael R Crowley, Elena I Frolova, Ilya Frolov

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2021. 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
2.4field-weighted citation impact, top 9% 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, 41 citations in OpenAlex.

  1. Article
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  7. Review
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  15. Glycosylation and the global virome.Molecular ecology · 2023
    Article
  16. Article
  17. Spike protein of SARS-CoV-2 variants: a brief review and practical implications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022
    Review
  18. Article
  19. Article
  20. SARS-CoV-2 Variants in Rhode Island; May 2022 Update.Rhode Island medical journal (2013) · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Nikita ShiliaevDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.
Tetyana LukashDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.
Oksana PalchevskaDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.
David K CrossmanUAB Genomics Core Facility, Department of Genetics, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.
Todd J GreenDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.ORCID 0000-0003-1158-4710
Michael R CrowleyUAB Genomics Core Facility, Department of Genetics, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.
Elena I FrolovaDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.ORCID 0000-0001-6523-9336
Ilya FrolovDepartment of Microbiology, University of Alabama at Birminghamgrid.265892.2, Birmingham, Alabama, USA.ORCID 0000-0002-8548-2517
University of Alabama at Birmingham · US

Funding

Tissue and organ specific human B cell immunity: Supplement - Metabolic Risk Factors and Inflammation in PASC DevelopmentU19AI142737 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI TECTOR, MATTHEW F. · 2019 to 2023
$19.7M
Mechanistic role of ns2 protein in evasion of innate immune response by alphavirusesR01AI133159 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOVA, ELENA I · 2017 to 2021
$3.0M
Alphavirus nsP3 protein: roles of intrinsically disordered region in virus replication and pathogenesisR01AI118867 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOVA, ELENA I · 2015 to 2019
$1.8M
Mechanistic understanding of SH3 domain-containing protein function in alphavirus replicationR21AI146969 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI FROLOV, ILYA V. · 2019 to 2020
$401k
HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01AI118867HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R01AI133159HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) R21AI146969HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) U19AI142737NIAID NIH HHS R01 AI118867NIAID NIH HHS R01 AI133159NIAID NIH HHS R21 AI146969NIAID NIH HHS U19 AI142737
6 · The paper itself

Abstract

One of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virulence factors is the ability to interact with high affinity to the ACE2 receptor, which mediates viral entry into cells. The results of our study demonstrate that within a few passages in cell culture, both the natural isolate of SARS-CoV-2 and the recombinant cDNA-derived variant acquire an additional ability to bind to heparan sulfate (HS). This promotes a primary attachment of viral particles to cells before their further interactions with the ACE2. Interaction with HS is acquired through multiple mechanisms. These include (i) accumulation of point mutations in the N-terminal domain (NTD) of the S protein, which increases the positive charge of the surface of this domain, (ii) insertions into the NTD of heterologous peptides containing positively charged amino acids, and (iii) mutation of the first amino acid downstream of the furin cleavage site. This last mutation affects S protein processing, transforms the unprocessed furin cleavage site into the heparin-binding peptide, and makes viruses less capable of syncytium formation. These viral adaptations result in higher affinity of viral particles to heparin, dramatic increase in plaque sizes, more efficient viral spread, higher infectious titers, and 2 orders of magnitude higher infectivity. The detected adaptations also suggest an active role of NTD in virus attachment and entry. As in the case of other RNA-positive (RNA

Indexed as

Evolution, MolecularAdaptation, BiologicalAnimalsBinding SitesChlorocebus aethiopsCytopathogenic Effect, ViralDNA, ComplementaryFurinHeparan SulfateHeparinHost-Pathogen InteractionsProtein BindingProtein DomainsProtein Processing, Post-TranslationalSARS-CoV-2Serial PassageDNA, ComplementaryFurinHeparan SulfateHeparinSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2coronavirusfurin cleavageheparin bindingrecombinant virusSARS-CoV-2spike NTDspike proteinviral evolution

Identifiers

PMID34406867
PMCPMC8513475
OpenAlexW3195693708

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.