TITLE

The CDw65 Monoclonal Antibodies VIM-8 and VIM-11 Bind to the Neutral Glycolipid V3FucnLc8Cer

AUTHOR(S)
Kniep, Bernhard; Peter-Katalinic, Jasna; Miithing, Johannes; Komatsu, Yasuhiko; Majdic, Otto; Pickl, Winfried F.; Knapp, Walter
PUB. DATE
January 1996
SOURCE
Journal of Biochemistry;1996, Vol. 119 Issue 3, p456
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
At the IVth and Vth Workshop on Human Leukocyte Differentiation Antigens a group of monoclonal antibodies recognizing myeloid cells was found to bind to the ganglioside X3- NeuAcVII3FucnLe10Cer (VIM-2 dodecasaccharide). 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 molecular and the cellular level. Binding of VIM-2 is abolished after treatment of cells with Vibrio cholerae neuramlnidase, whereas VTM-8 and VIM-11 show enhanced binding to neuraminidase-treated cells. We investigated binding of the three mAbs to glycolipid antigens with shorter carbohydrate chains. Distinct differences were observed in the binding of CDw65 antibodies to VIII3- NeuAcVII3FucnLe10Cer (VIM-2 decasaccharide). VIM-2 strongly bound to this antigen, whereas no binding was observed with the other two mAbs. Conversely, the asialoganglioside of the VIM-2 decasaceharide, V3FucnLe8Cer, 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.
ACCESSION #
80117180

 

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