Evidence map›Paper›PMID 10400774›Full record

ArticleJournal of virology1999

Structure of adenovirus complexed with its internalization receptor, alphavbeta5 integrin.

C Y Chiu, P Mathias, G R Nemerow, P L Stewart

Abstract read
In one paragraph

Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Article
  2. Review
  3. NgR1 binding to reovirus reveals an unusual bivalent interaction and a new viral attachment protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Biomedical nanoparticle design: What we can learn from viruses.Journal of controlled release : official journal of the Controlled Release Society · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

10 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

4 authors.

C Y ChiuDepartment of Molecular and Medical Pharmacology, Crump Institute for Biological Imaging, University of California-Los Angeles School of Medicine, Los Angeles, California 90095, USA.
P Mathias
G R Nemerow
P L Stewart

Funding

UCLA-Caltech Medical Scientist Training ProgramT32GM008042 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI AJIJOLA, OLUJIMI A, DAWSON, DAVID WAYNE · 1985 to 2023
$29.9M
AV INTEGRINS AND ADENOVIRUS INTERNALIZATIONR01HL054352 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1995 to 2016
$7.5M
ROLE OF CELL INTEGRINS IN ADENOVIRAL CONJUNCTIVITISR01EY011431 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1997 to 2012
$4.9M
Cryo-EM Structural Studies of Adenovirus Cell EntryR01AI042929 · NIAID · VANDERBILT UNIVERSITY · PI STEWART, PHOEBE L · 2004 to 2010
$2.8M
CRYO-EM STRUCTURAL STUDIES OF ADENOVIRUS CELL ENTRYR29AI042929 · NIAID · VANDERBILT UNIVERSITY · PI STEWART, PHOEBE L · 1997 to 2001
$214k
NEI NIH HHS EY11431NEI NIH HHS R01 EY011431NHLBI NIH HHS HL54352NHLBI NIH HHS R01 HL054352NIAID NIH HHS AI42929NIAID NIH HHS R01 AI042929NIAID NIH HHS R29 AI042929NIGMS NIH HHS T32 GM008042
6 · The paper itself

Abstract

The three-dimensional structure of soluble recombinant integrin alphavbeta5 bound to human adenovirus types 2 and 12 (Ad2 and -12) has been determined at approximately 21-A resolution by cryoelectron microscopy (cryo-EM). The alphavbeta5 integrin is known to promote Ad cell entry. Cryo-EM has shown that the integrin-binding RGD (Arg-Gly-Asp) protrusion of the Ad2 penton base protein is highly mobile (P. L. Stewart, C. Y. Chiu, S. Huang, T. Muir, Y. Zhao, B. Chait, P. Mathias, and G. R. Nemerow, EMBO J. 16:1189-1198, 1997). Sequence analysis indicated that the Ad12 RGD surface loop is shorter than that of Ad2 and probably less flexible, hence more suitable for structural characterization of the Ad-integrin complex. The cryo-EM structures of the two virus-receptor complexes revealed a ring of integrin density above the penton base of each virus serotype. As expected, the integrin density in the Ad2 complex was diffuse while that in the Ad12 complex was better defined. The integrin consists of two discrete subdomains, a globular domain with an RGD-binding cleft approximately 20 A in diameter and a distal domain with extended, flexible tails. Kinetic analysis of Ad2 interactions with alphavbeta5 indicated approximately 4.2 integrin molecules bound per penton base at close to saturation. These results suggest that the precise spatial arrangement of five RGD protrusions on the penton base promotes integrin clustering and the signaling events required for virus internalization.

Indexed as

Capsid ProteinsCryoelectron MicroscopyReceptors, VitronectinAdenoviruses, HumanAntibodies, ViralCapsidHumansIntegrinsKineticsReceptors, VirusSolubilityVirionAntibodies, ViralCapsid Proteinsintegrin alphaVbeta5Integrinspenton protein, adenovirusReceptors, VirusReceptors, Vitronectin

Identifiers

PMID10400774
PMCPMC112761

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.