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(Received for publication, April 4, 1995) From the The entire surface of the cercarial stage of the human blood
fluke Schistosoma mansoni is covered by a 1-µm thick,
highly immunogenic, fucose-rich glycocalyx (GCX). Using strategies
based on enzymatic, chemical, and mass spectrometric analysis, we have
defined the structures of the major glycans released by reductive
elimination from GCX. They comprise a heterogeneous population of
multifucosylated complex oligosaccharides with the following
nonreducing terminal sequences:
Our structural data suggest
that these tri- to pentafucosylated epitopes are carried on type 1,
R
Volume 270,
Number 29,
Issue of July 21, pp. 17114-17123, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
1
4GlcNAc
1
3Gal
1- Motif Constitutes
the Repeating Unit of the Complex O-Glycans Derived from the
Cercarial Glycocalyx of Schistosoma mansoni
Gal
13GalNAc, and type 2,
R
Gal
13(R
GlcNAc
16)GalNAc, core
structures via repeat units of
(3GalNAc
14(Fuc
12Fuc
12Fuc
13)GlcNAc
13Gal
)
,
where n is mainly 0 and 1, and all sugars are in the pyranose
form. The proposed structure represents the first instance where an
-galactosylated -GalNAc(14)-
-GlcNAc sequence
occurs as a repeating unit in a glycoprotein. It is also unique in
being substituted with oligofucosyl appendages. The unusual
oligosaccharide structures described here, particularly the potentially
immunodominant oligofucosyl moieties, are most likely responsible for
the known potency of GCX in modulating various immune responses
including complement activation, B cell mitogenesis, and delayed type
hypersensitivity in schistosomiasis.
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