Robustness of virus removal by protein A chromatography is independent of media lifetime.
The robustness of virus clearance with respect to protein A media reuse was demonstrated using media with four matrix chemistries: Protein A immobilized ProSep A, Poros A50, Protein A ceramic Hyper DF and MabSelect SuRe, an alkali resistant protein A ligand. Endogenous retrovirus clearance, step yield, impurity clearance and other performance parameters were evaluated periodically in media cycled up to 300 times. Media lifetime was generally limited by either declining step yield or media fouling. However, clearance of endogenous retrovirus remained in an acceptable range, either increasing or remaining constant. Multiply cycled media were tested for clearance of three viruses (SV40, X-MuLV, and MMV); clearance was comparable to naïve media. Overall, virus clearance by protein A chromatography appears to be extremely robust with respect to media age.
Lute
Scott
S
Office of Biotechnology Products, Center for Drug Evaluation and Research, Food and Drug Administration, 10903 New Hampshire Avenue, Silver Spring, MD 20993, USA.
Norling
Lenore
L
Hanson
Michael
M
Emery
Rachel
R
Stinson
Denise
D
Padua
Kevin
K
Blank
Greg
G
Chen
Qi
Q
Brorson
Kurt
K
D000818:Animals; D016466:CHO Cells / Q000821:virology; D002853:Chromatography, Liquid / Q000379:methods*; D006224:Cricetinae; D003412:Cricetulus; D017743:Equipment Reuse; D008855:Microscopy, Electron, Scanning; D010316:Particle Size; D012190:Retroviridae / Q000302:isolation & purification; D012685:Sepharose / Q000031:analogs & derivatives* / Q000737:chemistry; D013205:Staphylococcal Protein A / Q000737:chemistry*
D013205:Staphylococcal Protein A; C042030:Staphylococcal protein A-sepharose; D012685:Sepharose