Glycobiology, Vol 8, 695-705, Copyright © 1998 by Society for Glycobiology
E Moreno, B Lanne, AM Vazquez, I Kawashima, T Tai, LE Fernandez, KA Karlsson, J Angstrom and R Perez
P3 is a mouse monoclonal antibody (mAb) that binds to several NeuGc-
containing gangliosides. It also reacts with antigens expressed in human
breast tumors (Vazquez et al. (1995) Hybridoma , 14, 551-556). In this
work, the binding specificity of P3 has been characterized in more detail
using a panel of glycolipids that included several disialylated
gangliosides and several chemical derivatives of NeuGc-GM3. The carboxyl
group and the nitrogen function of sialic acid were found to play important
roles in the antibody binding, whereas the glycerol tail appears to be
nonrelevant. Molecular modeling was used to analyze the binding data,
including the finding that P3 selectively recognizes the internal NeuGc in
GD3. For this purpose, conformational studies of GD3 were performed using
molecular dynamics. It was concluded that sialic acid binds the P3 antibody
through its upper face (the one on which the carboxyl group is exposed) and
the C4-C5 side of the sugar ring, whereas none or very little contact
between the galactose residue and the protein is evident. Conformational
analysis of GD3 revealed that, despite the large flexibility of the
NeuGcalpha8NeuGc linkage, the P3 binding epitope on the external sialic
acid is not well exposed for any of the possible conformations this linkage
can adopt, whereas the internal sialic acid presents the epitope in a
proper way for several of these conformations. As a final result, a
coherent picture of the epitope that fits the wide binding data was
obtained.
ORIGINAL ARTICLES
Delineation of the epitope recognized by an antibody specific for N- glycolylneuraminic acid-containing gangliosides
Center of Molecular Immunology, P.O. Box 16040, Havana 11600, Cuba, Institute of Medical Biochemistry, Goteborg University, Medicinaregatan 9A, S-413 90 Goteborg, Sweden.
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