Recognition of Type 1 Chain Oligosaccharides and Lacto-Series Glycolipids by an Antibody to Human Secretory Component

H. Yu, J.M. Sipes, J. Cashel, M.A. Bakos, R.M. Goldblum, D.D. Roberts, H Yu, J M Sipes, J Cashel, M A Bakos, R M Goldblum, D D Roberts

Index: Arch. Biochem. Biophys. 322(2) , 299-305, (1995)

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Abstract

Binding of the mouse IgM antibody 6C4 is lost after treatment of human free secretory component with peptide N-glycosidase F (Bakos et al. (1991) J. Immunol. 146, 162-168) or periodate, suggesting that asparagine-linked oligosaccharides contain the epitope recognized by this antibody. Inhibition of antibody binding to free secretory component by milk oligosaccharides established that lacto-N-tetraose is the minimum structure recognized by the antibody, but larger oligosaccharides with terminal Galβ1-3GlcNAc sequences bind with much higher affinity. Antibody binding is enhanced by substitution with the Lewis Fucα1-4 and is inhibited by Fucα1-2Gal substitution. Free secretory component, however, does not bind other antibodies that recognize Lea or Leb oligosaccharides, and binding is lost after digestion with a β-galactosidase that cleaves Galβ1-3 linkages but not after digestion with α-L-fucosidase. Therefore, the major epitope recognized by 6C4 on free secretory component is probably not an asparagine-linked Lea oligosaccharide. The antibody also binds to human milk lactoferrin, some human mucins, and lacto-series glycolipids including III4αFuc-lactotetraosyl ceramide and lactotetraosyl ceramide. Based on affinity chromatography of oligosaccharides released from free secretory component, the epitope recognized by antibody 6C4 is present on approximately 3.5% of the asparagine-linked oligosaccharides.