Evidence map›Paper›PMID 31739438›Full record

ArticleInternational journal of molecular sciences2019

rAAV Engineering for Capsid-Protein Enzyme Insertions and Mosaicism Reveals Resilience to Mutational, Structural and Thermal Perturbations.

Rebecca C Feiner, Julian Teschner, Kathrin E Teschner, Marco T Radukic, Tobias Baumann, Sven Hagen, Yvonne Hannappel, Niklas Biere, Dario Anselmetti, Katja M Arndt and 1 more

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. AAV capsid sites breakdown: large protein insertions impact on vector dynamics.Frontiers in bioengineering and biotechnology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Anticancer Activity of Reconstituted Ribonuclease S-Decorated Artificial Viral Capsid.Chembiochem : a European journal of chemical biology · 2022
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. 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

11 authors.

Rebecca C FeinerCellular and Molecular Biotechnology, Faculty of Technology, Bielefeld University, 33615 Bielefeld, Germany.ORCID 0000-0002-8784-0875
Julian TeschnerCellular and Molecular Biotechnology, Faculty of Technology, Bielefeld University, 33615 Bielefeld, Germany.ORCID 0000-0001-5852-2758
Kathrin E TeschnerCellular and Molecular Biotechnology, Faculty of Technology, Bielefeld University, 33615 Bielefeld, Germany.
Marco T RadukicCellular and Molecular Biotechnology, Faculty of Technology, Bielefeld University, 33615 Bielefeld, Germany.ORCID 0000-0001-8721-966X
Tobias BaumannBiocatalysis group, Department of Chemistry, Technische Universität Berlin, 10623 Berlin, Germany.ORCID 0000-0001-7480-7809
Sven HagenCO.DON AG, 10587 Berlin, Germany.
Yvonne HannappelPhysical and Biophysical Chemistry (PCIII), Department of Chemistry, Bielefeld University, 33615 Bielefeld, Germany.
Niklas BiereExperimental Biophysics and Applied Nanoscience, Physics Department, Bielefeld University, 33615 Bielefeld, Germany.
Dario AnselmettiExperimental Biophysics and Applied Nanoscience, Physics Department, Bielefeld University, 33615 Bielefeld, Germany.ORCID 0000-0002-8720-4369
Katja M ArndtMolecular Biotechnology, Institute for Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany.
Kristian M MüllerCellular and Molecular Biotechnology, Faculty of Technology, Bielefeld University, 33615 Bielefeld, Germany.ORCID 0000-0002-7914-0625

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recombinant adeno-associated viruses (rAAV) provide outstanding options for customization and superior capabilities for gene therapy. To access their full potential, facile genetic manipulation is pivotal, including capsid loop modifications. Therefore, we assessed capsid tolerance to modifications of the structural VP proteins in terms of stability and plasticity. Flexible glycine-serine linkers of increasing sizes were, at the genetic level, introduced into the 587 loop region of the VP proteins of serotype 2, the best studied AAV representative. Analyses of biological function and thermal stability with respect to genome release of viral particles revealed structural plasticity. In addition, insertion of the 29 kDa enzyme β-lactamase into the loop region was tested with a complete or a mosaic modification setting. For the mosaic approach, investigation of VP2 trans expression revealed that a Kozak sequence was required to prevent leaky scanning. Surprisingly, even the full capsid modification with β-lactamase allowed for the assembly of capsids with a concomitant increase in size. Enzyme activity assays revealed lactamase functionality for both rAAV variants, which demonstrates the structural robustness of this platform technology.

Indexed as

Genetic EngineeringMutationProtein ConformationRecombinant Fusion ProteinsCapsid ProteinsDependovirusDNA, ViralGene Expression Regulation, ViralGenetic VectorsHumansImaging, Three-DimensionalModels, MolecularStructure-Activity RelationshipTerminal Repeat SequencesTransduction, GeneticVirionCapsid ProteinsDNA, ViralRecombinant Fusion Proteinsadeno-associated-viruscapsid stabilityinverted terminal repeat (ITR)loop modificationβ-lactamase

Identifiers

PMID31739438
PMCPMC6887778

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.