Novel tools for functional analysis of CD11c: activation-specific, activation-independent, and activating antibodies

J Immunoassay Immunochem. 2008;29(1):42-57. doi: 10.1080/15321810701735062.

Abstract

Functions and binding properties of four CD11c-specific mAbs are described here. The mAb 496B stimulated, while 496K inhibited ligand binding of CD11c. The stimulatory mAb, 496B, as well as the inhibitory mAbs BU15 and 496 K appear to act allosterically, as they do not bind the CD11c I domain. The mAb 3.9 bound preferentially to activated forms of CD11c and the binding was divalent cation dependent. CD11c binding to 3.9 recapitulates many of the integrin-ligand interactions. Our data suggest that 3.9 is a competitive antagonist, BU15 and 496K are allosteric antagonists, and 496B is an allosteric agonist of CD11c. These mAbs provide a set of tools to study the functions of the dendritic cell marker, CD11c.

MeSH terms

  • Antibodies, Blocking / immunology
  • Antibodies, Monoclonal / immunology*
  • CD11c Antigen / analysis*
  • CD11c Antigen / immunology*
  • Cations, Divalent / chemistry
  • Humans

Substances

  • Antibodies, Blocking
  • Antibodies, Monoclonal
  • CD11c Antigen
  • Cations, Divalent