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Mietzsch M, Yu JC, Hsi J, et al. Structural Study of Aavrh.10 Receptor and Antibody Interactions. J Virol. 2021;95(23):e0124921doi: 10.1128/JVI.01249-21.
Mietzsch, M., Yu, J. C., Hsi, J., Chipman, P., Broecker, F., Fuming, Z., Linhardt, R. J., Seeberger, P. H., Heilbronn, R., McKenna, R., & Agbandje-McKenna, M. (2021). Structural Study of Aavrh.10 Receptor and Antibody Interactions. Journal of virology, 95(23), e0124921. https://doi.org/10.1128/JVI.01249-21
Mietzsch, Mario, et al. "Structural Study of Aavrh.10 Receptor and Antibody Interactions." Journal of virology vol. 95,23 (2021): e0124921. doi: https://doi.org/10.1128/JVI.01249-21
Mietzsch M, Yu JC, Hsi J, Chipman P, Broecker F, Fuming Z, Linhardt RJ, Seeberger PH, Heilbronn R, McKenna R, Agbandje-McKenna M. Structural Study of Aavrh.10 Receptor and Antibody Interactions. J Virol. 2021 Nov 09;95(23):e0124921. doi: 10.1128/JVI.01249-21. Epub 2021 Sep 22. PMID: 34549984; PMCID: PMC8577363.
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J Virol. 2021 Nov 09;95(23):e0124921. doi: 10.1128/JVI.01249-21. Epub 2021 Sep 22.

Structural Study of Aavrh.10 Receptor and Antibody Interactions.

Journal of virology

Mario Mietzsch, Jennifer C Yu, Jane Hsi, Paul Chipman, Felix Broecker, Zhang Fuming, Robert J Linhardt, Peter H Seeberger, Regine Heilbronn, Robert McKenna, Mavis Agbandje-McKenna

Affiliations

  1. Department of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, College of Medicine, University of Floridagrid.15276.37, Gainesville, Florida, USA.
  2. Department of Biomolecular Systems, Max-Planck Institute of Colloids and Interfaces, Potsdam, Germany.
  3. Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany.
  4. Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA.
  5. Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, Berlin, Germany.

PMID: 34549984 PMCID: PMC8577363 DOI: 10.1128/JVI.01249-21

Abstract

Recombinant adeno-associated virus (rAAV) vectors are one of the leading tools for the delivery of therapeutic genes in human gene therapy applications. For a successful transfer of their payload, the AAV vectors have to circumvent potential preexisting neutralizing host antibodies and bind to the receptors of the target cells. Both of these aspects have not been structurally analyzed for AAVrh.10. Here, cryo-electron microscopy and three-dimensional image reconstruction were used to map the binding site of sulfated

Keywords: AAVrh.10; adeno-associated virus; antibody; capsid; cryo-EM; galactose; gene therapy; glycan; keratan sulfate; receptors

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