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Recognition of type 1 chain oligosaccharides and lacto-series glycolipids by an antibody to human secretory component.

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 Gal beta 1-3GlcNAc sequences bind with much higher affinity. Antibody binding is enhanced by substitution with the Lewis Fuc alpha 1-4 and is inhibited by Fuc alpha 1-2Gal substitution. Free secretory component, however, does not bind other antibodies that recognize Le(a) or Leb oligosaccharides, and binding is lost after digestion with a beta-galactosidase that cleaves Gal beta 1-3 linkages but not after digestion with alpha-L-fucosidase. Therefore, the major epitope recognized by 6C4 on free secretory component is probably not an asparagine-linked Le(a) oligosaccharide. The antibody also binds to human milk lactoferrin, some human mucins, and lacto-series glycolipids including III4 alpha Fuc-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.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Yu H,Sipes JM,Cashel J,Bakos MA,Goldblum RM,Roberts DD

doi

10.1006/abbi.1995.1467

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

299-305

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(85)71467-1

journal_volume

322

pub_type

杂志文章

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