Evidence map›Paper›PMID 19144372›Full record

ArticleVirology2009

Adeno-associated virus-2 and its primary cellular receptor--Cryo-EM structure of a heparin complex.

Jason O'Donnell, Kenneth A Taylor, Michael S Chapman

Open access · greenAbstract read
In one paragraph

Article in Virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
4.2field-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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 120 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025
    Review
  6. AAV vector development, back to the future.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. High-Resolution Imaging of Human Viruses in Liquid Droplets.Advanced materials (Deerfield Beach, Fla.) · 2021
    Article

24 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

3 authors at 2 institutions in 1 country.

Jason O'DonnellInstitute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306-4380, USA.
Kenneth A Taylor
Michael S Chapman
Florida State University · USOregon Health & Science University · US

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 1985 to 2011
$17.6M
Structure-Function of AAV - a Viral Gene Therapy Vector.R01GM066875 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI CHAPMAN, MICHAEL S. · 2003 to 2016
$4.1M
PURCHASE OF A LARGE FORMAT CCD CAMERA FOR 3-D EM: INFECTIOUS DISEASES10RR020919 · NCRR · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 2005 to 2005
$240k
CryoEM Equipment Enhancements for Florida State UniversityS10RR024564 · NCRR · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 2008 to 2008
$178k
NCRR NIH HHS P41 RR001081NCRR NIH HHS P41 RR-01081NCRR NIH HHS S10 RR020919NCRR NIH HHS S10 RR024564NIGMS NIH HHS R01 GM066875NIGMS NIH HHS R01 GM 66875
6 · The paper itself

Abstract

Adeno-associated virus serotype 2 (AAV-2) is a leading candidate vector for gene therapy. Cell entry starts with attachment to a primary receptor, Heparan Sulfate Proteoglycan (HSPG) before binding to a co-receptor. Here, cryo-electron microscopy provides direct visualization of the virus-HSPG interactions. Single particle analysis was performed on AAV-2 complexed with a 17 kDa heparin fragment at 8.3 A resolution. Heparin density covers the shoulder of spikes surrounding viral 3-fold symmetry axes. Previously implicated, positively charged residues R(448/585), R(451/588) and R(350/487) from another subunit cluster at the center of the heparin footprint. The footprint is much more extensive than apparent through mutagenesis, including R(347/484), K(395/532) and K(390/527) that are more conserved, but whose roles have been controversial. It also includes much of a region proposed as a co-receptor site, because prior studies had not revealed heparin interactions. Heparin density bridges over the viral 3-fold axes, indicating multi-valent attachment to symmetry-related binding sites.

Indexed as

CapsidCell MembraneCryoelectron MicroscopyDependovirusHeLa CellsHeparan Sulfate ProteoglycansHeparinHumansImage Processing, Computer-AssistedMicroscopy, ElectronModels, MolecularProtein Structure, TertiaryReceptors, Cell SurfaceReceptors, VirusHeparan Sulfate ProteoglycansHeparinheparin receptorReceptors, Cell SurfaceReceptors, Virus

Identifiers

PMID19144372
PMCPMC2684845
OpenAlexW1974638173

What OpenQuestion holds

Textmetadata
LicenceTDM
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.