Key result
Cryo-electron microscopy revealed that the capsid structures of AAV8, AAVrh.10, and AAVrh.39 are highly similar, suggesting specific residues S269 and N472 may confer blood-brain barrier crossing ability.
Why the study?
Capsid structural characterization at atomic resolution was needed for AAV8, AAVrh.10, and AAVrh.39 to provide knowledge for regulatory approval and vector engineering.
Population
AAVrh.10, AAVrh.39, and AAV8 capsid structures
Comparison
Comparative analysis of AAVrh.10, AAVrh.39, and AAV8
Design
Cryo-electron microscopy and image reconstruction structural study
Authors
Loading...
Structural insights into AAVrh.39 may inform capsid engineering; leaves open functional validation for clinical gene therapy applications.
Atomic resolution structural characterization of AAV vectors provides a platform for engineering improved receptor retargeting and tissue specificity for gene therapy.
Mietzsch et al. (2019) studied this question. AAVrh.10, AAVrh.39, and AAV8 capsids was evaluated on Capsid structure resolution. Cryo-electron microscopy revealed that the capsid structures of AAV8, AAVrh.10, and AAVrh.39 are highly similar, suggesting specific residues S269 and N472 may confer blood-brain barrier crossing ability.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: