Evidence map›Paper›PMID 34509611›Full record

ArticleJournal of structural biology2021

Comparative structural, biophysical, and receptor binding study of true type and wild type AAV2.

Antonette Bennett, Joshua Hull, Nelly Jolinon, Julie Tordo, Katie Moss, Enswert Binns, Mario Mietzsch, Cathleen Hagemann, R Michael Linden, Andrea Serio and 7 more

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Review
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

17 authors.

Antonette BennettDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Joshua HullDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Nelly JolinonDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London SE1 9RT, UK.
Julie TordoHandl Therapeutics, 3000 Leuven, Belgium.
Katie MossDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Enswert BinnsDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Mario MietzschDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Cathleen HagemannCentre for Craniofacial & Regenerative Biology, King's College London, London SE19RT, UK; The Francis Crick Institute, London NW1 1AT, UK.
R Michael LindenHandl Therapeutics, 3000 Leuven, Belgium.
Andrea SerioCentre for Craniofacial & Regenerative Biology, King's College London, London SE19RT, UK; The Francis Crick Institute, London NW1 1AT, UK.
Paul ChipmanDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Duncan SousaBiological Science Imaging Resource, Department of Biological Sciences, Florida State University, 89 Chieftan Way Rm 119, Tallahassee, FL 32306, USA.
Felix BroeckerDepartment of Biomolecular Systems, Max-Planck-Institute of Colloids and Interfaces, 14476 Potsdam, Germany.
Peter SeebergerInstitute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.
Els HenckaertsDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, London SE1 9RT, UK; Laboratory of Viral Cell Biology and Therapeutics, Department of Cellular and Molecular Medicine, Department of Microbiology, Immunology and Transplantation, KU Leuven, 3000 Leuven, Belgium. Electronic address: els.henckaerts@kuleuven.be.
Robert McKennaDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA. Electronic address: mckenna@ufl.edu.
Mavis Agbandje-McKennaDepartment of Biochemistry & Molecular Biology, Center for Structural Biology, The McKnight Brain Institute, College of Medicine, University of Florida, Gainesville, FL 32610, USA.

Funding

Structural studies of AAV capsids and their glycan receptor interactionsR01GM082946 · NIGMS · UNIVERSITY OF FLORIDA · PI ROBERT MCKENNA · 2007 to 2026
$6.1M
The Southeastern Consortium for Microscopy of MacroMolecular MachinesU24GM116788 · NIGMS · FLORIDA STATE UNIVERSITY · PI AGBANDJE-MCKENNA, MAVIS, BULLITT, ESTHER · 2016 to 2020
$4.6M
Purchase of a FEI Titan Krios for 3-D EMS10RR025080 · NCRR · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 2008 to 2008
$2.0M
Purchase of a direct electron camera for the Titan-Krios at FSUS10OD018142 · OD · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 2014 to 2014
$384k
Medical Research Council MR/S009302/1NCRR NIH HHS S10 RR025080NIGMS NIH HHS R01 GM082946NIGMS NIH HHS U24 GM116788NIH HHS S10 OD018142
6 · The paper itself

Abstract

Adeno-associated viruses (AAV) are utilized as gene transfer vectors in the treatment of monogenic disorders. A variant, rationally engineered based on natural AAV2 isolates, designated AAV-True Type (AAV-TT), is highly neurotropic compared to wild type AAV2 in vivo, and vectors based on it, are currently being evaluated for central nervous system applications. AAV-TT differs from AAV2 by 14 amino acids, including R585S and R588T, two residues previously shown to be essential for heparan sulfate binding of AAV2. The capsid structures of AAV-TT and AAV2 visualized by cryo-electron microscopy at 3.4 and 3.0 Å resolution, respectively, highlighted structural perturbations at specific amino acid differences. Differential scanning fluorimetry (DSF) performed at different pH conditions demonstrated that the melting temperature (T

Indexed as

Mutagenesis, Site-DirectedAnimalsBinding SitesCapsidCapsid ProteinsCell Line, TumorCryoelectron MicroscopyDependovirusGenetic VectorsHeLa CellsHumansMiceModels, MolecularProtein ConformationSf9 CellsSpodopteraCapsid ProteinsAAV-TTAntibody bindingcryo-EMGlycan arrayReceptor bindingStability

Identifiers

PMID34509611
PMCPMC9918372

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.