Comparative study of blood group-recognizing lectins toward ABO blood group antigens on neoglycoproteins, glycoproteins and complex-type oligosaccharides

• Published in: Biochimica et biophysica acta 2001-02, Vol.1525 (1), p.50-57
• Main Authors: Matsui, Taei, Hamako, Jiharu, Ozeki, Yasuhiro, Titani, Koiti
• Format: Article
• Language: English
• Subjects: ABO blood group; ABO Blood-Group System - chemistry; ABO Blood-Group System - immunology; ABO Blood-Group System - metabolism; Adult; Animals; Carbohydrate Sequence; Complex-type oligosaccharide; Glycoproteins - chemistry; Glycoproteins - immunology; Glycoproteins - metabolism; Helix pomatia agglutinin; Humans; In Vitro Techniques; Lectin; Lectins - metabolism; Molecular Sequence Data; Mucins - chemistry; Mucins - immunology; Mucins - metabolism; Oligosaccharides - chemistry; Oligosaccharides - immunology; Oligosaccharides - metabolism; Ulex europaeus agglutinin I; Von Willebrand factor; von Willebrand Factor - chemistry; von Willebrand Factor - immunology; von Willebrand Factor - metabolism
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(00)00170-7

Binding specificities of ABO blood group-recognizing lectins toward blood group antigens on neoglycoproteins, glycoproteins and complex-type oligosaccharides were studied by lectin-blotting analysis, enzyme linked immunosorbent assay and lectin-conjugated agarose column chromatography. Human serum albumin conjugated with A- and B-trisaccharides was clearly recognized by Helix pomatia (HPA), Phaseolus lunatus, Dolichos biflorus agglutinins, and Griffonia simplicifolia I agglutinin B 4, respectively. Almost the same results were obtained for human group A and B ovarian cyst and A-active hog gastric mucins, but Glycine max agglutinin only reacted to the group A hog mucin. When human plasma von Willebrand factor (vWF), having Asn-linked blood group antigens, was tested, HPA was highly sensitive to blood group A antigen on the vWF. Ulex europaeus agglutinin I (UEA-I) preferentially bound to the vWF from blood group O plasma. Within the GalNAc-recognizing lectins examined, a biantennary complex-type oligosaccharide having the blood group A structure retarded on an HPA–agarose column, and the affinity was diminished after digestion with α- N-acetylgalactosaminidase. This product bound to UEA-I agarose column. These results indicate that HPA and UEA-I are most sensitive for detection of glycoproteins possessing small amounts of blood group A and H antigens and also useful for fractionation of complex-type oligosaccharides with blood group A and H antigens, respectively.