Monoclonal antibody capture and viral clearance by cation exchange chromatography

Biotechnol Bioeng. 2012 Aug;109(8):2048-58. doi: 10.1002/bit.24480. Epub 2012 Apr 8.


Traditionally, post-production culture harvest capture of therapeutic monoclonal antibodies (mAbs) is performed using Protein A chromatography. We investigated the efficiency and robustness of cation exchange chromatography (CEX) in an effort to evaluate alternative capture methodologies. Up to five commercially available CEX resins were systematically evaluated using an experimentally optimized buffer platform and a design-of-experiment (DoE) approach for their ability to (a) capture a model mAb with a neutral isoelectric point, (b) clear three model viruses (porcine parvovirus, CHO type-C particles, and a bacteriophage). This approach identified a narrow operating space where yield, purity, and viral clearance were optimal under a CEX capture platform, and revealed trends between viral clearance of PPV and product purity (but not yield). Our results suggest that after unit operation optimization, CEX can serve as a suitable capture step.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / chemistry
  • Antibodies, Monoclonal / isolation & purification*
  • Biotechnology / methods*
  • Chromatography, Ion Exchange / methods*
  • Isoelectric Point
  • Viruses / isolation & purification


  • Antibodies, Monoclonal