THE CDW65 MONOCLONAL-ANTIBODIES VIM-8 AND VIM-11 BIND TO THE NEUTRAL GLYCOLIPID V(3)FUCNLC(8)CER

At the IVth and V-th Workshop On Human Leukocyte Differentiation Antig ens a group of monoclonal antibodies recognizing myeloid cells was fou nd to bind to the ganglioside X(3)-NeuAcVII(3)FucnLc(10)Cer (VIM-2 dod ecasaccharide), These antibodies were given the provisional cluster of differentiation designation CDw65. Three antibodies of this cluster ( VIM-2, VIM-8, and VIM-11) have now been studied in detail at the molec ular and the cellular level, Binding of VIM-2 is abolished after treat ment of cells with Vibrio cholerae neuraminidase, whereas VIM-8 and VI M-11 show enhanced binding to neuraminidase-treated cells. We investig ated binding of the three mAbs to glycolipid antigens with shorter car bohydrate chains, Distinct differences were observed in the binding of CDw65 antibodies to VIII(3)NeuAcV(3)FucnLc(8)Cer (VIM-2 decasaccharid e). VIM-2 strongly bound to this antigen, whereas no binding was obser ved with the other two mAbs, Conversely, the asialoganglio-side of the VIM-2 decasaccharide, V(3)FucnLc(8)Cer, was not recognized by VIM-2, but this antigen bound strongly VIM-8 and VIM-11, Thus, VIM-2 and the other CDw65 antibodies represented two different antigen specificities .