Evidence map›Paper›PMID 38190651›Full record

ArticleThe journal of physical chemistry. B2024

Two Receptor Binding Strategy of SARS-CoV-2 Is Mediated by Both the N-Terminal and Receptor-Binding Spike Domain.

Michele Monti, Edoardo Milanetti, Myrthe T Frans, Mattia Miotto, Lorenzo Di Rienzo, Maksim V Baranov, Giorgio Gosti, Arun Kumar Somavarapu, Madhu Nagaraj, Thaddeus W Golbek and 9 more

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.4field-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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Missense mutations on SynGAP C2 domain impair membrane diffusion.Protein science : a publication of the Protein Society · 2026
    Article
  4. Human coronavirus HKU1 neutralization by glycan receptor mimicry.bioRxiv : the preprint server for biology · 2025
    Article
  5. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  6. Polysialosides Outperform Sulfated Analogs for Binding with SARS-CoV-2.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Review
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

19 authors at 4 institutions in 3 countries.

Michele MontiRNA Systems Biology, Centre for Human Technologies (CHT), Istituto Italiano di Tecnologia (IIT), Via Enrico Melen, 83, 16152 Genova, Italy.
Edoardo MilanettiCenter for Life Nanoscience, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161 Rome, Italy.ORCID 0000-0002-3046-5170
Myrthe T FransMolecular Immunology─Groningen Biomolecular Sciences and Biotechnology, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Mattia MiottoCenter for Life Nanoscience, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161 Rome, Italy.
Lorenzo Di RienzoCenter for Life Nanoscience, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161 Rome, Italy.
Maksim V BaranovMolecular Immunology─Groningen Biomolecular Sciences and Biotechnology, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Giorgio GostiCenter for Life Nanoscience, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161 Rome, Italy.
Arun Kumar SomavarapuInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.
Madhu NagarajInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.
Thaddeus W GolbekDepartment of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.ORCID 0000-0002-3632-2701
Emiel RossingSynthetic Organic Chemistry, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.ORCID 0000-0002-6381-6475
Sam J MoonsSynthetic Organic Chemistry, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.ORCID 0000-0001-5507-3811
Thomas J BoltjeSynthetic Organic Chemistry, Radboud University Nijmegen, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.ORCID 0000-0001-9141-8784
Geert van den BogaartMolecular Immunology─Groningen Biomolecular Sciences and Biotechnology, Nijenborgh 7, 9747 AG Groningen, The Netherlands.ORCID 0000-0003-2180-6735
Tobias WeidnerDepartment of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.ORCID 0000-0002-7083-7004
Daniel E OtzenInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C, Denmark.ORCID 0000-0002-2918-8989
Gian Gaetano TartagliaRNA Systems Biology, Centre for Human Technologies (CHT), Istituto Italiano di Tecnologia (IIT), Via Enrico Melen, 83, 16152 Genova, Italy.ORCID 0000-0001-7524-6310
Giancarlo RuoccoCenter for Life Nanoscience, Istituto Italiano di Tecnologia, Viale Regina Elena 291, 00161 Rome, Italy.
Steven J RoetersDepartment of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark.ORCID 0000-0003-3238-2181
Italian Institute of Technology · ITAarhus University · DKRadboud University Nijmegen · NLUniversity of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is not well understood why severe acute respiratory syndrome (SARS)-CoV-2 spreads much faster than other β-coronaviruses such as SARS-CoV and Middle East respiratory syndrome (MERS)-CoV. In a previous publication, we predicted the binding of the N-terminal domain (NTD) of SARS-CoV-2 spike to sialic acids (SAs). Here, we experimentally validate this interaction and present simulations that reveal a second possible interaction between SAs and the spike protein via a binding site located in the receptor-binding domain (RBD). The predictions from molecular-dynamics simulations and the previously-published 2D-Zernike binding-site recognition approach were validated through flow-induced dispersion analysis (FIDA)─which reveals the capability of the SARS-CoV-2 spike to bind to SA-containing (glyco)lipid vesicles, and flow-cytometry measurements─which show that spike binding is strongly decreased upon inhibition of SA expression on the membranes of angiotensin converting enzyme-2 (ACE2)-expressing HEK cells. Our analyses reveal that the SA binding of the NTD and RBD strongly enhances the infection-inducing ACE2 binding. Altogether, our work provides

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2Binding SitesHumansProtein BindingAngiotensin-Converting Enzyme 2

Identifiers

PMID38190651
PMCPMC10801686
OpenAlexW4390658640

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.