Interaction of Artocarpus lectins with human IgA does not involve asparagine-linked oligosaccharide of the immunoglobulin.
In view of the controversy with respect to the interaction of jacalin with human IgA2, a study was undertaken to assess the reactivity of the Artocarpus heterophyllus lectin, as well as the lectin from Artocarpus integer (lectin C), with subclasses of human immunoglobulin A by ELISA. Our data is consistent with the view that Artocarpus lectins have no affinity for the IgA2 immunoglobulins. In further support of the findings, we have established that N-linked oligosaccharide moieties of IgA have no significant bearing in the lectin-immunoglobulin binding. Interaction was also not affected in the presence of 1% (w/v) BSA.
Hashim
O H
OH
Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur.
Kobayashi
K
K
Taniguchi
N
N
D000581:Amidohydrolases / Q000378:metabolism; D015295:Antigens, Tumor-Associated, Carbohydrate; D001216:Asparagine; D002240:Carbohydrate Sequence; D004187:Disaccharides / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D007070:Immunoglobulin A / Q000145:classification / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D008553:Melibiose / Q000494:pharmacology; D008969:Molecular Sequence Data; D009194:Myeloma Proteins / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism*; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D037121:Plant Lectins; D012710:Serum Albumin, Bovine / Q000494:pharmacology
D015295:Antigens, Tumor-Associated, Carbohydrate; D004187:Disaccharides; D007070:Immunoglobulin A; D037102:Lectins; D009194:Myeloma Proteins; D009844:Oligosaccharides; D037121:Plant Lectins; C043696:jacalin; D012710:Serum Albumin, Bovine; C016467:Thomsen-Friedenreich antigen; D001216:Asparagine; D008553:Melibiose; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase