Evidence map›Paper›PMID 32992715›Full record

ArticleViruses2020

Binding Mechanism Elucidation of the Acute Respiratory Disease Causing Agent Adenovirus of Serotype 7 to Desmoglein-2.

Marc-André Hograindleur, Gregory Effantin, Daphna Fenel, Caroline Mas, André Lieber, Guy Schoehn, Pascal Fender, Emilie Vassal-Stermann

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed, 1 pooled it
1.3field-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

9 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. EPsInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
    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

8 authors at 2 institutions in 2 countries.

Marc-André HograindleurUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.ORCID 0000-0002-7558-0279
Gregory EffantinUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.
Daphna FenelUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.
Caroline MasUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.
André LieberDepartment of Medicine, Division of Medical Genetics, University of Washington, Seattle, WA 98195, USA.
Guy SchoehnUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.ORCID 0000-0002-1459-3201
Pascal FenderUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.ORCID 0000-0002-6698-3367
Emilie Vassal-StermannUniv. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France.ORCID 0000-0002-8486-4935
Centre National de la Recherche Scientifique · FRUniversity of Washington Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of viruses causing acute respiratory distress syndromes (ARDS) is more essential than ever at a time when a virus can create a global pandemic in a matter of weeks. Among human adenoviruses, adenovirus of serotype 7 (HAdV7) is one of the most virulent serotypes. This virus regularly re-emerges in Asia and has just been the cause of several deaths in the United States. A critical step of the virus life cycle is the attachment of the knob domain of the fiber (HAd7K) to the cellular receptor desmoglein-2 (DSG2). Complexes between the fiber knob and two extracellular domains of DSG2 have been produced. Their characterization by biochemical and biophysical methods show that these two domains are sufficient for the interaction and that the trimeric HAd7K could accommodate up to three DSG2 receptor molecules. The cryo-electron microscopy (cryo-EM) structure of these complexes at 3.1 Å resolution confirmed the biochemical data, and allowed the identification of the critical amino acid residues for this interaction, which shows similarities with other DSG2 interacting adenoviruses, despite a low homology in the primary sequences.

Indexed as

Adenoviridae InfectionsAdenoviruses, HumanCapsid ProteinsCryoelectron MicroscopyDesmoglein 2HEK293 CellsHost-Pathogen InteractionsHumansModels, MolecularMutationProtein BindingProtein ConformationReceptors, VirusRespiratory Distress SyndromeSerogroupCapsid ProteinsDesmoglein 2DSG2 protein, humanhexon capsid protein, AdenovirusReceptors, Virusacute respiratory distress syndromesadenovirusescryo-electron microscopydesmoglein-2virus-host interactions

Identifiers

PMID32992715
PMCPMC7599583
OpenAlexW3088861931

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.