Evidence map›Paper›PMID 39976108›Full record

ArticleAnalytical chemistry2025

Variant-Specific Interactions at the Plasma Membrane: Heparan Sulfate's Impact on SARS-CoV-2 Binding Kinetics.

Dario Valter Conca, Fouzia Bano, Małgorzata Graul, Julius von Wirén, Lauriane Scherrer, Hudson Pace, Himanshu Sharma, Justas Svirelis, Konrad Thorsteinsson, Andreas Dahlin and 1 more

Abstract read
In one paragraph

Article in Analytical chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–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

6 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. 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

11 authors.

Dario Valter ConcaDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.ORCID 0000-0002-7640-6387
Fouzia BanoDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.ORCID 0000-0003-0634-7091
Małgorzata GraulDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.
Julius von WirénDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.
Lauriane ScherrerDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.
Hudson PaceDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.ORCID 0000-0001-5116-2577
Himanshu SharmaWallenberg Centre for Molecular Medicine (WCMM), Umeå University, Umeå 901 87, Sweden.
Justas SvirelisDepartment of Chemistry and Chemical Engineering, Chalmers University of Technology, Gothenburg 412 96, Sweden.
Konrad ThorsteinssonDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.
Andreas DahlinDepartment of Chemistry and Chemical Engineering, Chalmers University of Technology, Gothenburg 412 96, Sweden.ORCID 0000-0003-1545-5860
Marta BallyDepartment of Clinical Microbiology, Umeå University, Umeå 901 87, Sweden.ORCID 0000-0002-5865-8302

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spread of SARS-CoV-2 led to the emergence of several variants of concern (VOCs). The spike glycoprotein, responsible for engaging the viral receptor, exhibits the highest density of mutations, suggesting an ongoing evolution to optimize viral entry. This study characterizes the bond formed by virion mimics carrying the SARS-CoV-2 spike protein and the plasma membrane of host cells in the early stages of virus entry. Contrary to the traditional analysis of isolated ligand-receptor pairs, we utilized well-defined biomimetic models and biochemical and biophysical techniques to characterize the multivalent interaction of VOCs with the complex cell membrane. We observed an overall increase in the binding affinity for newer VOCs. By progressively reducing the system complexity, we identify heparan sulfate (HS) as a main driver of this variation, with a 10-fold increase in affinity for Omicron BA.1 over that of the original strain. These results demonstrate the essential role of coreceptors, particularly HS, in the modulation of SARS-CoV-2 infection and highlight the importance of multiscale biophysical and biochemical assays that account for membrane complexity to fully characterize and understand the role of molecular components and their synergy in viral attachment and entry.

Indexed as

Cell MembraneHeparan SulfateSARS-CoV-2Spike Glycoprotein, CoronavirusCOVID-19HumansKineticsProtein BindingVirus InternalizationHeparan SulfateSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID39976108
PMCPMC11883730

What OpenQuestion holds

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Registered trials

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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.