Evidence map›Paper›PMID 30862836›Full record

ArticleNature communications2019

CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement.

Emilie Vassal-Stermann, Gregory Effantin, Chloe Zubieta, Wim Burmeister, Frédéric Iseni, Hongjie Wang, André Lieber, Guy Schoehn, Pascal Fender

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

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  19. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
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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

9 authors at 3 institutions in 2 countries.

Emilie Vassal-StermannInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France.
Gregory EffantinInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France.
Chloe ZubietaLaboratoire de Physiologie Cellulaire et Végétale, Biosciences and Biotechnology Institute of Grenoble, UMR5168, CNRS/CEA/INRA/UGA, 17 Rue des Martyrs, 38054, Grenoble, France.
Wim BurmeisterInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France.ORCID http://orcid.org/0000-0003-0876-6118
Frédéric IseniUnité de Virologie, Institut de Recherche Biomédicale des Armées, BP 73, 91223, Brétigny-sur-Orge Cedex, France.
Hongjie WangDepartment of Medicine, Division of Medical Genetics, University of Washington, Box 357720, Seattle, WA, 98195, USA.
André LieberDepartment of Medicine, Division of Medical Genetics, University of Washington, Box 357720, Seattle, WA, 98195, USA. lieber00@u.washington.edu.
Guy SchoehnInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France.ORCID http://orcid.org/0000-0002-1459-3201
Pascal FenderInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France. pascal.fender@ibs.fr.ORCID http://orcid.org/0000-0002-6698-3367
Centre National de la Recherche Scientifique · FRUniversity of Washington Medical Center · USInstitut de Virologie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Attachment of human adenovirus (HAd) to the host cell is a critical step of infection. Initial attachment occurs via the adenoviral fibre knob protein and a cellular receptor. Here we report the cryo-electron microscopy (cryo-EM) structure of a <100 kDa non-symmetrical complex comprising the trimeric HAd type 3 fibre knob (HAd3K) and human desmoglein 2 (DSG2). The structure reveals a unique stoichiometry of 1:1 and 2:1 (DSG2: knob trimer) not previously observed for other HAd-receptor complexes. We demonstrate that mutating Asp261 in the fibre knob is sufficient to totally abolish receptor binding. These data shed new light on adenovirus infection strategies and provide insights for adenoviral vector development and structure-based design.

Indexed as

Virus AttachmentAdenoviridae InfectionsAdenoviruses, HumanAsparagineCapsid ProteinsCryoelectron MicroscopyDesmoglein 2HEK293 CellsHumansModels, MolecularProtein DomainsReceptors, VirusRecombinant ProteinsAsparagineCapsid ProteinsDesmoglein 2DSG2 protein, humanhexon capsid protein, AdenovirusReceptors, VirusRecombinant Proteins

Identifiers

PMID30862836
PMCPMC6414520
OpenAlexW2952220348

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.