Novel tools for functional analysis of CD11c: activation-specific, activation-independent, and activating antibodies.
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.
Sadhu
Chanchal
C
ICOS Corporation, Bothell, WA 98021, USA. csadhu@comcast.net
Hendrickson
Lee
L
Dick
Ken O
KO
Potter
Tamara G
TG
Staunton
Donald E
DE
D019138:Antibodies, Blocking / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology*; D039521:CD11c Antigen / Q000032:analysis* / Q000276:immunology*; D002413:Cations, Divalent / Q000737:chemistry; D006801:Humans
D019138:Antibodies, Blocking; D000911:Antibodies, Monoclonal; D039521:CD11c Antigen; D002413:Cations, Divalent