Evidence map›Paper›PMID 38613462›Full record

ArticleChembiochem : a European journal of chemical biology2024

SARS-CoV-2 Spike Protein-Derived Cyclic Peptides as Modulators of Spike Interaction with GRP78.

Nicholas Johnson, Craig Pattinson, Kate Burgoyne, Karolin Hijazi, Wael E Houssen, Bruce F Milne

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  3. Review
  4. 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

6 authors at 1 institution in 2 countries.

Nicholas JohnsonInstitute of Medical Sciences, University of Aberdeen, Ashgrove Road West, Aberdeen, AB25 2ZD, UK.ORCID https://orcid.org/0000-0001-6608-4348
Craig PattinsonSchool of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, AB25 2ZD, UK.ORCID https://orcid.org/0009-0003-8735-1603
Kate BurgoyneSchool of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, AB25 2ZD, UK.ORCID https://orcid.org/0000-0003-3986-0975
Karolin HijaziSchool of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, AB25 2ZD, UK.ORCID https://orcid.org/0000-0002-8589-2129
Wael E HoussenInstitute of Medical Sciences, University of Aberdeen, Ashgrove Road West, Aberdeen, AB25 2ZD, UK.ORCID https://orcid.org/0000-0001-9653-5111
Bruce F MilneDepartment of Chemistry, University of Aberdeen, Meston Walk, Aberdeen, AB24 3UE, UK.ORCID https://orcid.org/0000-0002-5522-4808
University of Aberdeen · GB

Funding

BBSRC BB/V509206/1EPSRC EP/S027246/1GCRF Covid-19 ResponseIBioIC CTP PhDLaboratory for Advanced Computing of the University of CoimbraPortuguese FCT-Fundação UIDB/04564/2020Portuguese FCT-Fundação UIDP/04564/2020Portuguese National Network for Advanced Computing 2021.09804.CPCA
6 · The paper itself

Abstract

The human glucose-regulated protein GRP78 is a human chaperone that translocactes to the cell surface when cells are under stress. Theoretical studies suggested it could be involved in SARS-CoV-2 virus entry to cells. In this work, we used in vitro surface plasmon resonance-based assays to show that human GRP78 indeed binds to SARS-CoV-2 spike protein. We have designed and synthesised cyclic peptides based on the loop structure of amino acids 480-488 of the SARS-CoV-2 spike protein S1 domain from the Wuhan and Omicron variants and showed that both peptides bind to GRP78. Consistent with the greater infectiousness of the Omicron variant, the Omicron-derived peptide displays slower dissociation from the target protein. Both peptides significantly inhibit the binding of wild-type S1 protein to the human protein GRP78 suggesting that further development of these cyclic peptide motifs may provide a viable route to novel anti-SARS-CoV-2 agents.

Indexed as

Endoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsPeptides, CyclicSARS-CoV-2Spike Glycoprotein, CoronavirusCOVID-19HumansProtein BindingEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanPeptides, CyclicSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2BiPCyclic peptidesGRP78HSPA5SARS-CoV-2

Identifiers

PMID38613462
PMCPMC11497264
OpenAlexW4394783493

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.