Evidence map›Paper›PMID 17010669›Full record

ArticleMolecular therapy : the journal of the American Society of Gene Therapy2006

Proteolytic mapping of the adeno-associated virus capsid.

Kim Van Vliet, Veronique Blouin, Mavis Agbandje-McKenna, Richard O Snyder

Open access · bronzeAbstract read
In one paragraph

Article in Molecular therapy : the journal of the American Society of Gene Therapy, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

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  16. Inner limiting membrane barriers to AAV-mediated retinal transduction from the vitreous.Molecular therapy : the journal of the American Society of Gene Therapy · 2009
    Article
  17. Article
  18. Article
  19. The role of the adeno-associated virus capsid in gene transfer.Methods in molecular biology (Clifton, N.J.) · 2008
    Review
  20. Article
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 at 3 institutions in 2 countries.

Kim Van VlietDepartment of Molecular Genetics and Microbiology, University of Florida, College of Medicine, 1600 SW Archer Road, Gainesville, FL 32610-0266, USA.
Veronique Blouin
Mavis Agbandje-McKenna
Richard O Snyder
Pediatrics and Genetics · USFlorida College · USMolecular Biology Consortium · US

Funding

VIRAL VECTOR DELIVERY OF ANTISENSE TO ACE MRNA IN CARDIOVASCULAR DISEASEP01HL059412 · NHLBI · UNIVERSITY OF FLORIDA · PI MUZYCZKA, NICHOLAS · 1998 to 2012
$20.2M
Vector CoreP01HL051811 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI GUGGINO, WILLIAM B. · 1993 to 2013
$20.2M
NHLBI NIH HHS P01 HL051811NHLBI NIH HHS P01 HL051811-119004NHLBI NIH HHS P01 HL059412NHLBI NIH HHS P01 HL059412-079001NHLBI NIH HHS P01 HL51811NHLBI NIH HHS P01 HL59412
6 · The paper itself

Abstract

The three-dimensional structures of the viral capsid of three AAV serotypes have previously been determined by X-ray crystallography or cryoelectron microscopy. These studies of AAV and similar studies of autonomous parvoviruses have yielded important structural information about the virions in a low-energy conformation. However, there is little information on the structural properties of AAV virions in solution under physiological conditions. We demonstrate that proteolytic digestion of AAV2 virions with trypsin results in cleavage at a specific site on the capsid surface while the capsid remains intact. The products of digestion were mapped using unique antibodies, protein sequencing, mass spectroscopy, and 3D structure modeling to a region on a surface loop that is common to all three AAV2 structural proteins. Empty AAV2 capsids could be distinguished from full (DNA-containing) capsids, having an increased susceptibility of VP2 to trypsin and being digested more rapidly by chymotrypsin. Proteolytic analysis utilizing trypsin or chymotrypsin was also capable of distinguishing AAV2 from AAV1 and AAV5, as seen by differential susceptibility and unique fragment patterns. These data demonstrate a novel approach for studying the structure of AAV capsids in solution and should be valuable in the testing and engineering of AAV vectors for gene transfer.

Indexed as

Amino Acid SequenceBlotting, WesternCapsidCapsid ProteinsChymotrypsinDependovirusElectrophoresis, Polyacrylamide GelEndopeptidasesHeparinImmunoblottingMicroscopy, Electron, TransmissionModels, MolecularProtein Structure, SecondaryProtein Structure, TertiaryTrypsinViral ProteinsCapsid ProteinsChymotrypsinEndopeptidasesHeparinTrypsinViral Proteins

Identifiers

PMID17010669
PMCPMC1808542
OpenAlexW2111526115

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.