The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine.
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.
Prenner
C
C
Institut für Chemie, Universität für Bodenkultur, Vienna, Austria.
Mach
L
L
Glössl
J
J
März
L
L
D000117:Acetylglucosamine / Q000378:metabolism*; D001216:Asparagine / Q000378:metabolism; D001514:Bee Venoms / Q000201:enzymology*; D015153:Blotting, Western; D002241:Carbohydrates / Q000276:immunology*; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D005643:Fucose / Q000378:metabolism*; D006023:Glycoproteins / Q000276:immunology; D006031:Glycosylation; D010741:Phospholipases A / Q000276:immunology*; D054467:Phospholipases A2; D010944:Plants / Q000378:metabolism
D001514:Bee Venoms; D002241:Carbohydrates; D000939:Epitopes; D006023:Glycoproteins; D005643:Fucose; D001216:Asparagine; D010741:Phospholipases A; D054467:Phospholipases A2; D000117:Acetylglucosamine