Evidence map›Paper›PMID 33744314›Full record

ArticleJournal of molecular biology2021

SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on Ca

Alex L Lai, Jack H Freed

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation.International journal of molecular sciences · 2025
    Article
  6. Machine and deep learning to predict viral fusion peptides.Computational and structural biotechnology journal · 2025
    Article
  7. Making the cut: Multiscale simulation of membrane remodeling.Current opinion in structural biology · 2024
    Review
  8. SARS-CoV-2 pathogenesis in an angiotensin II-induced heart-on-a-chip disease model and extracellular vesicle screening.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
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  14. Review
  15. Article
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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

2 authors at 1 institution in 1 country.

Alex L LaiACERT, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, United States.
Jack H FreedACERT, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, United States. Electronic address: jhf3@cornell.edu.
Cornell University · US

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
Electron Spin Relaxation in Model MembranesR01GM123779 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2017 to 2020
$2.1M
X/Q Band Pulsed ENDOR SpectrometerS10OD021543 · OD · CORNELL UNIVERSITY · PI FREED, JACK H · 2016 to 2016
$1.4M
NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R01 GM123779NIH HHS S10 OD021543
6 · The paper itself

Abstract

Coronaviruses are a major infectious disease threat, and include the zoonotic-origin human pathogens SARS-CoV-2, SARS-CoV, and MERS-CoV (SARS-2, SARS-1, and MERS). Entry of coronaviruses into host cells is mediated by the spike (S) protein. In our previous ESR studies, the local membrane ordering effect of the fusion peptide (FP) of various viral glycoproteins including the S of SARS-1 and MERS has been consistently observed. We previously determined that the sequence immediately downstream from the S2' cleavage site is the bona fide SARS-1 FP. In this study, we used sequence alignment to identify the SARS-2 FP, and studied its membrane ordering effect. Although there are only three residue differences, SARS-2 FP induces even greater membrane ordering than SARS-1 FP, possibly due to its greater hydrophobicity. This may be a reason that SARS-2 is better able to infect host cells. In addition, the membrane binding enthalpy for SARS-2 is greater. Both the membrane ordering of SARS-2 and SARS-1 FPs are dependent on Ca

Indexed as

Amino Acid SequenceBinding SitesCalciumCalorimetryCell MembraneHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsSARS-CoV-2Severe acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusThermodynamicsViral Fusion ProteinsVirus InternalizationCalciumSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, SARS-CoV-2Viral Fusion ProteinsCOVID-19ESRhydrophobicityion specificityITC

Identifiers

PMID33744314
PMCPMC7969826
OpenAlexW3137974527

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.