Recent advances in cryo-electron microscopy have yielded a library of currently ∼150 high-resolution AAV capsid structures, with more than 50% determined in the last 5 years alone.
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AAV capsid structures
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Recent cryo-electron microscopy advances have produced about 150 high-resolution AAV capsid structures, with more than half determined in the last 5 years.
AAV capsid structures and complexes with receptors, purification agents, and antibodies have been instrumental for rational capsid engineering and guide design of variants with enhanced transduction efficiency, tissue specificity, and reduced detection by pre-existing neutralizing antibodies.
Structural studies of AAV capsids over about 25 years have improved understanding of AAV biology and informed their use as gene therapy vectors for human disease treatment.
Comparative analyses of primate and nonprimate AAV capsids reveal conserved architecture including the canonical jelly-roll fold and surface variations that affect receptor interaction, antibody recognition, and intracellular trafficking.