The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of α1,3-fucosylation of the asparagine-bound N-acetylglucosamine

Author:

Prenner C1,Mach L2,Glössl J2,März L1

Affiliation:

1. Institut für Chemie, Universität für Bodenkultur, Gregor-Mendelstrasse 33, A- 1180 Vienna, Austria

2. Zentrum für Angewandte Genetik, Universität für Bodenkultur, Gregor-Mendelstrasse 33, A- 1180 Vienna, Austria

Abstract

A rabbit polyclonal antiserum raised against honey-bee (Apis mellifera) venom phospholipase A2 (PLA2) contains antibodies that react exclusively with its glycosylated variants and cross-react with plant glycoproteins. The interaction of anti-(horseradish peroxidase) antiserum with PLA2 suggests the existence of a carbohydrate determinant common to both glycoproteins. E.l.i.s.a. binding and inhibition experiments, employing glycoproteins and glycopeptides of plant and animal origin with known N-glycan structures, in combination with chemical and enzymic deglycosylation, identified alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine as the antigenic determinant. This fucose residue is present in the N-glycan of PLA2 and is frequently found in plant glycoproteins, whereas mammalian glycoproteins lack this modification.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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