Inhibition of processing of asparagine-linked carbohydrate chains on IgG2a by using swainsonine has no influence upon antibody effector functions in vitro.
Removal of asparagine (Asn)-linked carbohydrate chains from IgG antibody molecules reduces their antibody effector functions such as C activation and FcR binding. We have prepared IgG2a mAb with modified structure of carbohydrate chains by treating the hybridoma cells with swainsonine, which inhibits the processing of Asn-linked carbohydrate chains at the site of action of mannosidase II. These antibodies have obtained the capacity to bind lentil lectin and have become sensitive to endoglycosidase H digestion, indicating the structural changes of oligosaccharides from complex type to hybrid type. They behaved in an identical manner to the normal IgG2a antibodies with regards to extracellular secretion, Ag-binding capacity, C-mediated hemolysis and FcR-mediated functions. Critical moieties of Asn-linked carbohydrate chains on IgG molecules to retain their antibody effector functions were discussed.
Nose
M
M
Department of Pathology, Tohoku University School of Medicine, Sendai, Japan.
Heyman
B
B
D000118:Acetylglucosaminidase / Q000494:pharmacology; D000470:Alkaloids / Q000494:pharmacology*; D000818:Animals; D000906:Antibodies / Q000276:immunology; D001216:Asparagine / Q000032:analysis; D002241:Carbohydrates / Q000502:physiology*; D007074:Immunoglobulin G / Q000276:immunology / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism; D008361:Mannosidases / Q000037:antagonists & inhibitors*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D051379:Mice; D037121:Plant Lectins; D013329:Structure-Activity Relationship; D017026:Swainsonine
D000470:Alkaloids; D000906:Antibodies; D002241:Carbohydrates; D007074:Immunoglobulin G; D037102:Lectins; D037121:Plant Lectins; C033619:lentil lectin; D001216:Asparagine; D008361:Mannosidases; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D017026:Swainsonine