Reaction of Antimannan Antibodies with Oligomannosides and Glycopeptides1

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Abstract
A number of oligomannosides and glycopeptides prepared from various sources were tested for their potency to inhibit the binding of 3H-mannotetraitol (Manα1→3Manα1→3→2Manα1→3→ 2Mannitol) to antimannan antibodies. It was found that antimannan antibodies are highly specific to the Manα1→3→3Man structure, reacting very poorly with the Manα1→3→2Man and Manα1→6Man structures. A Manα1→3man structure at the non-reducing end is far more reactive than one at an inner position. In this respect, antimannan antibodies differ from concanavalin A which reacts with mannose residues substituted at C−2 as well as those at non-reducing ends. Glycopeptides prepared from ovalbumin, Taka amylase A and from membrane glycoproteins of rat liver cross-reacted with antimannan antibodies to various extents reflecting the characteristic structures of the individual glycopeptides.