Open AccessMonoclonal antibodies that block cell adhesion in Polysphondylium pallidum : reaction with L ‐fucose, a terminal sugar in cell‐surface glycoproteins
Author(s) -
TODA Katsumi,
THARANATHAN Rudrapatham N.,
BOZZARO Salvatore,
GERISCH Günther
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08395.x
Subject(s) - fucose , glycoprotein , oligosaccharide , monoclonal antibody , chemistry , mannose , biochemistry , antibody , microbiology and biotechnology , biology , immunology
By permethylation analysis the linkages of L ‐fucose and D ‐mannose in the oligosaccharide residues of cell surface glycoproteins of Polysphondylium pallidum were determined. Mannose was found in terminal positions, in 1,2‐, 1,3‐ and 1,6‐intra‐chain linkages, and at branch points. Fucose was exclusively located at nonreducing ends. Fab of a monoclonal antibody, mAb 293, has been previously shown to inhibit cell adhesion in P. pallidum completely. Binding of this antibody to glycoprotein was blocked by L ‐fucose, and at very high concentrations also by D ‐mannose. The dissociation constant for the antibody‐fucose complex was K d = 70μM, which was two orders of magnitude higher than estimated for the natural oligosaccharide. Antibody‐glycoprotein complexes dissociated in the presence of 100 mM L ‐fucose with a half‐time of about 56s. The blockage by L ‐fucose is taken as evidence that the adhesion‐blocking antibody binds to oligosaccharide end groups containing L ‐fucose as the terminal sugar.