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- W1480541661 abstract "To directly evaluate the utility of distinct serotypes of adeno-associated virus (AAV) for gene therapy applications, it will be necessary to purify each in a similar manner. The methodology to obtain highly purified rAAV2 for use in clinical trials has been established using heparin column affinity binding in conjunction with iodixanol gradients. With the exception of AAV3, the other serotypes of AAV do not bind heparin. Recently the amino acids responsible for the ability of AAV2 to bind to heparin were identified (Kern et al 2003, J Virol 77:11072–81) and tested in the context of rAAV5 (Opie et al 2003, J Virol 77:6995–7006). To assess whether all serotypes could be modified to bind heparin, the AAV2 amino acids R585 R588 and A590 were substituted into the homologous positions in serotypes 1, 3, 4, and 5 to generate the pxr1RRA, pxr3RRA, pxr4RRA, and pxr5RRA plasmids. These helper vectors were then used to produce recombinant eGFP virus which were initially purified by either cesium chloride or iodixanol gradients followed by dialysis." @default.
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- W1480541661 date "2004-05-01" @default.
- W1480541661 modified "2023-09-26" @default.
- W1480541661 title "Universal purification of AAV serotypes 1–5 modified to contain a heparin binding epitope" @default.
- W1480541661 doi "https://doi.org/10.1016/j.ymthe.2004.06.026" @default.
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