Structure of the AAVhu.37 capsid by cryoelectron microscopy.

Publisher: John Wiley & Sons Inc Country of Publication: United States NLM ID: 101620319 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2053-230X (Electronic) Linking ISSN: 2053230X NLM ISO Abbreviation: Acta Crystallogr F Struct Biol Commun Subsets: MEDLINE

Original Publication: Malden, MA : John Wiley & Sons Inc., [2014]-

Mutation* ; Protein Conformation*; Capsid/*ultrastructure ; Cryoelectron Microscopy/*methods ; Dependovirus/*chemistry ; Genetic Vectors/*chemistry; Crystallography, X-Ray ; Dependovirus/genetics ; Genetic Vectors/genetics ; Humans ; Models, Molecular

Adeno-associated viruses (AAVs) are used as in vivo gene-delivery vectors in gene-therapy products and have been heavily investigated for numerous indications. Over 100 naturally occurring AAV serotypes and variants have been isolated from primate samples. Many reports have described unique properties of these variants (for instance, differences in potency, target cell or evasion of the immune response), despite high amino-acid sequence conservation. AAVhu.37 is of interest for clinical applications owing to its proficient transduction of the liver and central nervous system. The sequence identity of the AAVhu.37 VP1 to the well characterized AAVrh.10 serotype, for which no structure is available, is greater than 98%. Here, the structure of the AAVhu.37 capsid at 2.56 Å resolution obtained via single-particle cryo-electron microscopy is presented.

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Keywords: AAVhu.37; adeno-associated viruses; capsid; cryo-EM structure; gene therapy; gene-delivery vectors

Date Created: 20200211 Date Completed: 20201112 Latest Revision: 20231113

20240829

PMC7010358

10.1107/S2053230X20000308

32039886