Evidence map›Paper›PMID 34365113›Full record

ReviewCurrent opinion in virology2021

Proteases and variants: context matters for SARS-CoV-2 entry assays.

Christian S Stevens, Kasopefoluwa Y Oguntuyo, Benhur Lee

Abstract readReview
In one paragraph

Review in Current opinion in virology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
–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

17 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Antigenic cartography using variant-specific hamster sera reveals substantial antigenic variation among Omicron subvariants.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Biology of the SARS-CoV-2 Coronavirus.Biochemistry. Biokhimiia · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
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

3 authors.

Christian S StevensDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, 10029, United States.
Kasopefoluwa Y OguntuyoDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, 10029, United States.
Benhur LeeDepartment of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, 10029, United States. Electronic address: benhur.lee@mssm.edu.

Funding

TRAINING PROGRAM: MECHANISMS OF VIRUS-HOST INTERACTIONST32AI007647 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI Domenico Tortorella · 2000 to 2026
$11.5M
Identification and Pre-Clinical Evaluation of Measles Virus InhibitorsR01AI071002 · NIAID · GEORGIA STATE UNIVERSITY · PI PLEMPER, RICHARD K. · 2006 to 2022
$6.6M
Efficient Sendai virus mediated CRISPR/Cas9 gene editing to protect hematopoietic stem cells from HIVR01AI138921 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AN, DONG SUNG, LEE, BENHUR · 2018 to 2022
$3.1M
Tropism, pathogenicity, and potential for zoonotic spillover of emergent henipa- and henipa-like virusesR01AI123449 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI LEE, BENHUR · 2016 to 2020
$2.7M
SUMO and ubiquitin modifications in henipavirus matrix trafficking and functionR01AI125536 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI LEE, BENHUR · 2016 to 2020
$2.1M
Functional interrogation of paramyxovirus genomes with efficient reverse geneticsR21AI115226 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI LEE, BENHUR · 2015 to 2016
$460k
Elucidating the molecular determinants of Henipavirus envelope-antibody and envelope-receptor interactions on viral entryF31AI154739 · NIAID · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI OGUNTUYO, KASOPEFOLUWA Y. · 2020 to 2022
$135k
NIAID NIH HHS F31 AI154739NIAID NIH HHS R01 AI071002NIAID NIH HHS R01 AI123449NIAID NIH HHS R01 AI125536NIAID NIH HHS R01 AI138921NIAID NIH HHS R21 AI115226NIAID NIH HHS T32 AI007647
6 · The paper itself

Abstract

Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), like other coronaviruses, relies on a flexible array of entry mechanisms, driven by the spike (S) protein. Entry is dependent on proteolytic priming, activation, and receptor binding; all of which can be variable, dependent on context. Here we review the implications of the complexity of SARS-CoV-2 entry pathways on entry assays that then drive our understanding of humoral immunity, therapeutic efficacy, and tissue restriction. We focus especially on the proteolytic activation of SARS-CoV-2 spike and how this constellation of proteases lends deeper insight to our understanding of arising variants and their putative role transmission or variable pathogenicity in vivo. In this review, we argue for better universal standards to assay virus entry as well as suggest best practices for reporting viral passage number, the cell line used, and proteases present, among other important considerations.

Indexed as

Virus InternalizationCOVID-19HumansMutationPeptide HydrolasesSARS-CoV-2Spike Glycoprotein, CoronavirusPeptide HydrolasesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID34365113
PMCPMC8302850

What OpenQuestion holds

Textmetadata
LicenceTDM
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.