Evidence map›Paper›PMID 22951835›Full record

ArticleJournal of virology2012

Conserved fiber-penton base interaction revealed by nearly atomic resolution cryo-electron microscopy of the structure of adenovirus provides insight into receptor interaction.

Changchun Cao, Xiaoyan Dong, Xiaobing Wu, Boyun Wen, Gang Ji, Lingpeng Cheng, Hongrong Liu

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Molecular Engineering of Virus Tropism.International journal of molecular sciences · 2024
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Adenovirus Structure: What Is New?International journal of molecular sciences · 2021
    Review
  9. Review
  10. Review
  11. Article
  12. A packing for A-form DNA in an icosahedral virus.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Review
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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

7 authors at 2 institutions in 1 country.

Changchun CaoCollege of Physics and Information Science and Key Laboratory of Low-dimensional Quantum Structures and Quantum Control of the Ministry of Education, Hunan Normal University, Changsha, Hunan, China.
Xiaoyan Dong
Xiaobing Wu
Boyun Wen
Gang Ji
Lingpeng Cheng
Hongrong Liu
Hunan Normal University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenovirus (Ad) cell attachment is initiated by the attachment of the fiber protein to a primary receptor (usually CAR or CD46). This event is followed by the engagement of the penton base protein with a secondary receptor (integrin) via its loop region, which contains an Arg-Gly-Asp (RGD) motif, to trigger virus internalization. To understand the well-orchestrated adenovirus cell attachment process that involves the fiber and the penton base, we reconstructed the structure of an Ad5F35 capsid, comprising an adenovirus type 5 (Ad5) capsid pseudotyped with an Ad35 fiber, at a resolution of approximately 4.2 Å. The fiber-penton base interaction in the cryo-electron microscopic (cryo-EM) structure of Ad5F35 is similar to that in the cryo-EM structure of Ad5, indicating that the fiber-penton base interaction of adenovirus is conserved. Our structure also confirms that the C-terminal segment of the fiber tail domain constitutes the bottom trunk of the fiber shaft. Based on the conserved fiber-penton base interaction, we have proposed a model for the interaction of Ad5F35 with its primary and secondary receptors. This model could provide insight for designing adenovirus gene delivery vectors.

Indexed as

AdenoviridaeAmino Acid SequenceCapsidCell MembraneCryoelectron MicroscopyGenetic VectorsHumansImaging, Three-DimensionalIntegrinsMembrane Cofactor ProteinModels, MolecularMolecular ConformationMolecular Sequence DataProtein BindingProtein ConformationProtein Structure, TertiaryIntegrinsMembrane Cofactor Protein

Identifiers

PMID22951835
PMCPMC3486510
OpenAlexW2059560924

What OpenQuestion holds

Textmetadata
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.