Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8

Adeno‐associated viruses (AAVs) are actively being developed for clinical gene‐therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue‐transduction interactio...

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Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-06, Vol.61 (6), p.558-561
Main Authors: Lane, Michael Douglas, Nam, Hyun-Joo, Padron, Eric, Gurda-Whitaker, Brittney, Kohlbrenner, Eric, Aslanidi, George, Byrne, Barry, McKenna, Robert, Muzyczka, Nicholas, Zolotukhin, Sergei, Agbandje-McKenna, Mavis
Format: Article
Language:English
Subjects:
adeno-associated viruses
Animals
Capsid - chemistry
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - isolation & purification
Cell Line
Cloning, Molecular - methods
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization - methods
Crystallization Communications
CRYSTALS
Dependovirus - chemistry
EFFICIENCY
gene therapy
Insecta
INTERACTIONS
LIVER
MONOMERS
parvovirus
PROTEINS
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
VECTORS
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - isolation & purification
X-Ray Diffraction
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Summary:Adeno‐associated viruses (AAVs) are actively being developed for clinical gene‐therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue‐transduction interactions. AAV8 is ∼80% identical to the more widely studied AAV2, but its liver‐transduction efficiency is significantly greater than that of AAV2 and other serotypes. The production, purification, crystallization and preliminary X‐ray crystallographic analysis of AAV8 viral capsids are reported. The crystals diffract X‐rays to 3.0 Å resolution using synchrotron radiation and belong to the hexagonal space group P6322, with unit‐cell parameters a = 257.5, c = 443.5 Å. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309105014132