A single-step affinity column for purification of serotype-5 based adeno-associated viral vectors.
Here we describe a single-step affinity column for purification of vectors based on adeno-associated virus type 5 (AAV5). A sialic-acid-rich protein called mucin was covalently attached to Sepharose and was found to bind AAV5 vectors. Elution with high salt efficiently recovered highly active vectors of greater purity than what is achieved with CsCl(2) sedimentation.
Auricchio
A
A
Institute for Human Gene Therapy, Department of Molecular and Cellular Engineering, University of Pennsylvania and The Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
O'Connor
E
E
Hildinger
M
M
Wilson
J M
JM
D000818:Animals; D002460:Cell Line; D002586:Cesium; D002712:Chlorides; D002846:Chromatography, Affinity / Q000379:methods*; D000229:Dependovirus / Q000145:classification* / Q000302:isolation & purification* / Q000378:metabolism / Q000502:physiology; D005822:Genetic Vectors / Q000302:isolation & purification*; D006801:Humans; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D009077:Mucins / Q000378:metabolism; D018482:Muscle, Skeletal / Q000821:virology; D012492:Salts / Q000494:pharmacology; D012685:Sepharose / Q000378:metabolism; D014461:Ultracentrifugation
D002712:Chlorides; D009077:Mucins; D012492:Salts; D002586:Cesium; D012685:Sepharose; C028019:cesium chloride