A case study on Sema3E-Fc aggregation and assay-dependent differences in quantitation

Bioanalysis. 2012 Mar;4(6):703-11. doi: 10.4155/bio.12.30.

Abstract

Background: In evaluating the serum concentrations in mice of a Sema3E IgG1 Fc fusion protein, a possible antitumor agent, two ELISAs were developed: a generic assay detecting only the Fc portion of the therapeutic and a specific receptor-binding assay detecting intact protein.

Results: An unexpected discrepancy was observed in the measured in vivo serum concentrations, with the generic ELISA yielding higher concentrations than the specific ELISA. Size-exclusion HPLC and SDS-PAGE analysis of in vitro serum stability samples revealed extensive aggregation of Sema3E-Fc. The generic assay recovered more Sema3E-Fc in the presence of aggregates than the specific assay.

Conclusion: Biophysical characterization combined with immunochemical analysis was key to elucidating not only the nature of the protein instability, but also the cause for the assay discrepancy.

MeSH terms

  • Animals
  • Antibodies / immunology
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay*
  • Female
  • Humans
  • Immunoglobulin Fc Fragments / genetics
  • Immunoglobulin Fc Fragments / immunology
  • Immunoglobulin Fc Fragments / metabolism*
  • Mice
  • Protein Stability
  • Recombinant Fusion Proteins / blood*
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Fusion Proteins / pharmacokinetics
  • Semaphorins / genetics
  • Semaphorins / immunology
  • Semaphorins / metabolism*
  • Time Factors

Substances

  • Antibodies
  • Immunoglobulin Fc Fragments
  • Recombinant Fusion Proteins
  • SEMA3E protein, human
  • Semaphorins