The interaction of selective plant lectins with neuraminidase-treated and untreated IgA1 from the sera of IgA nephropathy patients.
A study on the binding interaction of lectins from Artocarpus heterophyllus (jacalin), Glycine max and Sambucus nigra with standardised quantity of IgA from the IgA nephropathy patients and normal controls was performed. The Glycine max lectin demonstrated higher affinity towards the serum IgA of IgAN patients as compared to normal controls. However, the affinity binding was lower in cases ofjacalin and the Sambucus nigra lectin. When serum samples were treated with neuraminidase, the differential jacalin affinity binding between IgA1 of patients and normal controls was abrogated. Our data are in support of the view that the O-linked oligosaccharide moieties of the patients IgA1 were generally lacking in galactose and sialic acid residues.
Hashim
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OH
Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur.
Shuib
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AS
Chua
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CT
D000328:Adult; D001665:Binding Sites; D016022:Case-Control Studies; D005690:Galactose / Q000737:chemistry / Q000276:immunology; D005922:Glomerulonephritis, IGA / Q000276:immunology*; D006031:Glycosylation; D006801:Humans; D007070:Immunoglobulin A / Q000097:blood* / Q000737:chemistry; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism*; D008875:Middle Aged; D019158:N-Acetylneuraminic Acid / Q000737:chemistry / Q000276:immunology; D009439:Neuraminidase; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D030262:Soybean Proteins; D010835:Phytohemagglutinins
D005690:Galactose; D007070:Immunoglobulin A; D037102:Lectins; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D030262:Soybean Proteins; C050600:Sambucus nigra lectins; C043696:jacalin; C028824:soybean lectin; D010835:Phytohemagglutinins