Complexes with anti-epitope tag IgGs improve the therapeutic potential of epitope-tagged antibody fragments

Mol Immunol. 2010 Apr;47(7-8):1529-34. doi: 10.1016/j.molimm.2010.01.016. Epub 2010 Feb 12.

Abstract

The use of recombinant antibody fragments (rAbF) as therapeutic agents is compromised by shorter serum persistences than IgG therapeutics and their inability to mediate Fc-dependent effector functions. Here, we show that the strategy of complex formation between epitope-tagged rAbFs and anti-epitope IgG monoclonal antibodies (mAb) can improve the therapeutic potential of rAbFs by both enhancing their serum persistence and conferring on them the ability to recruit Fc-mediated effector functions. These two mechanistic aspects of this strategy were demonstrated using c-myc- and 6xHis-tagged Fab and scFv rAbFs, both directed against Pseudomonas aeruginosa O6ad, in combination with two different murine anti-epitope tag IgGs, anti-5xHis IgG (Penta-His) and anti-c-myc IgG (9E10). Further enhancement of this strategy for the employment of rAbFs as therapeutics is discussed.

MeSH terms

  • Animals
  • Antibodies, Anti-Idiotypic / immunology
  • Antibodies, Anti-Idiotypic / therapeutic use*
  • Antibodies, Monoclonal / immunology
  • Antibodies, Monoclonal / therapeutic use*
  • Cell Line
  • Epitopes / immunology*
  • Immunoglobulin Fragments / immunology
  • Immunoglobulin Fragments / therapeutic use*
  • Mice
  • Pseudomonas Infections / drug therapy*
  • Pseudomonas Infections / immunology
  • Pseudomonas aeruginosa / immunology*
  • Recombinant Proteins / immunology
  • Recombinant Proteins / therapeutic use

Substances

  • Antibodies, Anti-Idiotypic
  • Antibodies, Monoclonal
  • Epitopes
  • Immunoglobulin Fragments
  • Recombinant Proteins
  • anti-IgG