Monoclonal antibody specific to ?-2?3-linked deaminated neuraminyl ?-galactosyl sequence

1 February 1993

journal article
Published by Oxford University Press (OUP) in Glycobiology

Vol. 3 (1) , 31-36
https://doi.org/10.1093/glycob/3.1.31

Abstract

Fusion of spleen cells from a BALB/c mouse immunized with KDNα2→3Galβ1→4Glcβ1→1Cer ((KDN)G_M3) with P3-X63 Ag8.U1 (P3U1) mouse myeloma cells yielded a hybrid cell line that produced monoclonal antibody that bound to (KDN)G_M3, but not to Neu5Acα2→3Galβ1→4Glcβ1→1Cer ((Neu5Ac)G_M3). The specificity of the monoclonal antibody was determined chiefly by the enzyme-linked immunosorbent assay procedure. This antibody was found to react most strongly with (KDN)G_M3 and less strongly with a glycoprotein containing a number of KDNα2→3Galβ1→3GaINAcα1→3[(8KDNα2→)_n→6]GaINAcα1→ chains (<n>_av = ∼3). The results indicated that the monoclonal antibody (designated mAb.kdn3G) specifically and effectively recognized a disaccharide structure, KDNα2→3Galβ1→, and specifically discriminated (KDN)G_M3 from (Neu5Ac)G_M3. The mAb.kdn3G was used to localize (KDN)G_M3 in rainbow trout sperm by the indirect immunofluorescence procedure and the antigen was shown to be mostly, if not completely, associated with the external surface of the entire plasma membrane of rainbow trout sperm. The potential utility of mAb.kdn3G is addressed in searching for KDN-glyco-conjugates which contain glycan units having the KDNα2→3Galβ1→ epitope structure.

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