Evidence map›Paper›PMID 37122470›Full record

ArticleACS central science2023

Powerful Avidity with a Limited Valency for Virus-Attachment Blockers on DC-SIGN: Combining Chelation and Statistical Rebinding with Structural Plasticity of the Receptor.

Vanessa Porkolab, Martin Lepšík, Stefania Ordanini, Alexander St John, Aline Le Roy, Michel Thépaut, Emanuele Paci, Christine Ebel, Anna Bernardi, Franck Fieschi

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

17 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Virus-Mediated Self-Assembly of Functional Cyclodextrins for Antiviral Inhibition.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Covalent Activation of the C-type Lectin DC-SIGN.Angewandte Chemie (International ed. in English) · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Review
  13. Article
  14. Molecular recognition ofiScience · 2024
    Article
  15. Article
  16. Article
  17. 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

10 authors at 4 institutions in 4 countries.

Vanessa PorkolabUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France.
Martin LepšíkUniv. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France.
Stefania OrdaniniUniversita' degli Studi di Milano, Dipartimento di Chimica, via Golgi 19, 20133, Milano, Italy.
Alexander St JohnAstbury Centre & School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, United Kingdom.
Aline Le RoyUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France.
Michel ThépautUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France.
Emanuele PaciDepartment of Physics and Astronomy "Augusto Righi", University of Bologna, Via Zamboni, 33, 40126, Bologna, Italy.ORCID https://orcid.org/0000-0002-4891-2768
Christine EbelUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France.
Anna BernardiUniversita' degli Studi di Milano, Dipartimento di Chimica, via Golgi 19, 20133, Milano, Italy.ORCID https://orcid.org/0000-0002-1258-2007
Franck FieschiUniv. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, 38000 Grenoble, France.ORCID https://orcid.org/0000-0003-1194-8107
Centre National de la Recherche Scientifique · FRUniversity of Milan · ITUniversity of Bologna · ITUniversity of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-type lectin receptor DC-SIGN has been highlighted as the coreceptor for the spike protein of the SARS-CoV-2 virus. A multivalent glycomimetic ligand, Polyman26, has been found to inhibit DC-SIGN-dependent trans-infection of SARS-CoV-2. The molecular details underlying avidity generation in such systems remain poorly characterized. In an effort to dissect the contribution of the known multivalent effects - chelation, clustering, and statistical rebinding - we studied a series of dendrimer constructs related to Polyman26 with a rod core rationally designed to engage simultaneously two binding sites of the tetrameric DC-SIGN. Binding properties of these compounds have been studied with a range of biophysical techniques, including recently developed surface plasmon resonance oriented-surface methodology. Using molecular modeling we addressed, for the first time, the impact of the carbohydrate recognition domains' flexibility of the DC-SIGN tetramer on the compounds' avidity. We were able to gain deeper insight into the role of different binding modes, which in combination produce a construct with a nanomolar affinity despite a limited valency. This multifaceted experimental-theoretical approach provides detailed understanding of multivalent ligand/multimeric protein interactions which can lead to future predictions. This work opens the way to the development of new virus attachment blockers adapted to different C-type lectin receptors of viruses.

Identifiers

PMID37122470
PMCPMC10141607
OpenAlexW4321369367

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.