Robustness of virus removal by protein A chromatography is independent of media lifetime

J Chromatogr A. 2008 Sep 26;1205(1-2):17-25. doi: 10.1016/j.chroma.2008.07.094. Epub 2008 Aug 9.

Abstract

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.

MeSH terms

  • Animals
  • CHO Cells / virology
  • Chromatography, Liquid / methods*
  • Cricetinae
  • Cricetulus
  • Equipment Reuse*
  • Microscopy, Electron, Scanning
  • Particle Size
  • Retroviridae / isolation & purification
  • Sepharose / analogs & derivatives*
  • Sepharose / chemistry
  • Staphylococcal Protein A / chemistry*

Substances

  • Staphylococcal Protein A
  • Staphylococcal protein A-sepharose
  • Sepharose