Evidence map›Paper›PMID 31784892›Full record

ReviewMedical microbiology and immunology2020

Human adenovirus binding to host cell receptors: a structural view.

Aleksandra Cecylia Stasiak, Thilo Stehle

Abstract readReview
In one paragraph

Review in Medical microbiology and immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Postinfectious Bronchiolitis Obliterans in Children.Canadian respiratory journal · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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

2 authors.

Aleksandra Cecylia StasiakInterfaculty Institute of Biochemistry, University of Tübingen, Hoppe-Seyler-Str. 4, 72076, Tübingen, Germany.ORCID http://orcid.org/0000-0001-6914-5740
Thilo StehleInterfaculty Institute of Biochemistry, University of Tübingen, Hoppe-Seyler-Str. 4, 72076, Tübingen, Germany. thilo.stehle@uni-tuebingen.de.

Funding

H2020 Marie Skłodowska-Curie Actions (ViBrANT ITN) 765042
6 · The paper itself

Abstract

Human Adenoviruses (HAdVs) are a family of clinically and therapeutically relevant viruses. A precise understanding of their host cell attachment and entry mechanisms can be applied in inhibitor design and the construction of targeted gene delivery vectors. In this article, structural data on adenovirus attachment and entry are reviewed. HAdVs engage two types of receptors: first, an attachment receptor that is bound by the fibre knob protein protruding from the icosahedral capsid, and next, an integrin entry receptor bound by the pentameric penton base at the capsid vertices. Adenoviruses use remarkably diverse attachment receptors, five of which have been studied structurally in the context of HAdV binding: Coxsackie and Adenovirus Receptor, CD46, the glycans GD1a and polysialic acid, and desmoglein-2. Together with the integrin entry receptors, they display both symmetrical and asymmetrical modes of binding to the virus as demonstrated by the structural analyses reviewed here. The diversity of HAdV receptors contributes to the broad tropism of these viruses, and structural studies are thus an important source of information on HAdV-host cell interactions. The imbalance in structural data between the more and less extensively studied receptors remains to be addressed by future research.

Indexed as

Protein BindingVirus AttachmentVirus InternalizationAdenoviruses, HumanCoxsackie and Adenovirus Receptor-Like Membrane ProteinDesmoglein 2GangliosidesHost Microbial InteractionsHumansIntegrinsMembrane Cofactor ProteinReceptors, VirusSialic AcidsCD46 protein, humanCoxsackie and Adenovirus Receptor-Like Membrane ProteinDesmoglein 2ganglioside, GD1aGangliosidesIntegrinsMembrane Cofactor Proteinpolysialic acidReceptors, VirusSialic AcidsCryoelectron microscopyHuman adenovirusReviewStructural biologyX-ray crystallography

Identifiers

PMID31784892
PMCPMC7248032

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.