Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid‐containing Ser/Thr‐linked carbohydrate chains of N‐terminal octapeptides from human glycophorin A

Abstract

The interaction of the Maackia amurensis hemagglutinin (MAH) with various glycopeptides and oligosaccharides was investigated by means of immobilized lectin affinity chromatography.An amino terminal octapeptide obtained from human glycophorin A having three Neu5Aca2+3Gal/I1+3(Neu5Aca2+6)GalNAc tetrasaccharide chains, designated as CB-II, was found to have an extremely strong affinity for MAH. Therefore, it is strongly suggested that hemagglutination by MAH was caused by its interaction with Ser/Thr-linked carbohydrate chains of human glycophorin A on erythrocyte membranes.

Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing TerminalN-Acetylneuraminic Acid α2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans

“…Lectins that distinguish various linkages of sialic acid are elderberry bark lectin (SNA 1 ; Sambucus nigra agglutinin) (5), Japanese elderberry lectin (SSA; S. sieboldiana agglutinin) (6), and Polyporus squamosus lectin (7) that are specific for NeuAc␣2,6Gal/GalNAc sequences; Maackia amurensis mitogen (MAL) that reacts with greatest affinity to the trisaccharide sequence NeuAc/Gc␣2,3Gal␤1,4GlcNAc/Glc, which is usually present in N-linked oligosaccharides (8), and the hemagglutinin from the same source (MAH) that displays higher affinity for a disialylated tetrasaccharide found in the O-linked oligosaccharide, NeuAc␣2,3Gal␤1,3(NeuAc␣2,6)GalNAc␣ (9). In contrast to these sequence-specific lectins, wheat germ lectin (WGA) and Limax flavus lectin have been used as general tools to bind sialylated glycoconjugates (10,11).…”

Carbohydrate/glycan-binding specificity of legume lectins in respect to their proposed biological functions

“…Although the lectins are gifted of at least a monosacharidebinding site, it is reasonable to suppose that their biological ligand are larger than a single monosaccharide. Indeed, lectins not only bind to oligosacchaides, but this interaction is tighter than that to their monosacchaide inhibitor (Konami et al, 1994;Do & Lee, 1998;Dam et al, 1998). Although the ability to interact with oligosacchaide had been proved early, the first complex of a lectin with a complex glycan was established later by crystallographic studies (Bourne et al, 1990b(Bourne et al, , 1994Naismith et al, 1996).…”

“…The mannose specific lectins constitute a growing group of proteins from Monocotyledoneae plants, whose interaction is specially towards mannose, a fact not observed in glucose/mannose lectins (Chandra et al, 1999). In addition, lectins have been demonstrated to interact with syalic acid and some derivatives, although glucose and galactose specific lectins also show ability to interact with this acid (Konami et al, 1994). More recently, increasing efforts have been made to establish the physiological role of plant lectins and two distinct hypothesis has been placed on the evidence to explain how lectins are involved in the metabolism of their native plants (Van Damme et al, 1998).…”

In vivo modulated N‐acyl side chain of N‐acetylneuraminic acid modulates the cell contact‐dependent inhibition of growth

“…highly sialylated contac-60-tinhibin) was without significant effects, while membrane-lo-40-calized contactinhibin from sparse cells, which is also highly sialylated, consistently stimulated growth, suggesting the ex-20 , istence of membrane-localized species of contactinhibin in 1 1'0 60 sparse cells which differ structurally from highly sialylated eelle seeaea/.elltx lo3~ intracellular forms. [17] " and SNA [18], respectively. Fig.…”