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J Biol Chem, Vol. 275, Issue 12, 8625-8632, March 24, 2000
From the Glycobiology Research and Training Center and Department
of Medicine, University of California San Diego,
La Jolla, California 92093
The siglecs (sialic acid-binding
immunoglobulin superfamily
lectins) are immunoglobulin superfamily members
recognizing sialylated ligands. Most prior studies of siglec
specificities focused on
New Aspects of Siglec Binding Specificities, Including the
Significance of Fucosylation and of the Sialyl-Tn Epitope*
and
2-3- and 2-6-sialyllactos(amin)es and
on one or two of the siglecs at a time. Here, we explore several new
aspects of specificities of the first six reported siglecs, using
sialylated glycans presented in multivalent form, on synthetic
polyacrylamide backbones, or on mucin polypeptides. First, we report
that binding of siglec-1 (sialoadhesin), siglec-3 (CD33), siglec-4a
(myelin-associated glycoprotein), and siglec-5 to 2-3
sialyllactosamine is affected markedly by the presence of an
1-3-linked fucose. Thus, while siglecs may not interfere with
selectin-mediated recognition, fucosylation could negatively regulate
siglec binding. Second, in contrast to earlier studies, we find that
siglec-3 prefers 2-6-sialyllactose. Third, siglec-5 binds
2-8-linked sialic acid, making it the siglec least specific for
linkage recognition. Fourth, siglecs-2 (CD22), -3, -5, and -6 (obesity-binding protein 1) showed significant binding to sialyl-Tn
(Neu5Ac2-6-GalNAc), a tumor marker associated with poor prognosis.
Fifth, siglec-6 is an exception among siglecs in not requiring the
glycerol side chain of sialic acid for recognition. Sixth, all siglecs
require the carboxyl group of sialic acid for binding. Finally, the
presentation of the sialyl-Tn epitope and/or more extended structures
that include this motif may be important for optimal recognition by the
siglecs. This was concluded from studies using ovine, bovine, and
porcine submaxillary mucins and Chinese hamster ovary cells transfected with ST6GalNAc-I and/or the mucin polypeptide MUC1.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of long term fellowship from the Human Frontier Science Program.
§
Supported by United States Public Health Service Grants P01 HL57345
and R01GM3273. To whom correspondence should be addressed: Glycobiology
Research and Training Center, CMM East, UC San Diego, La Jolla, CA
92093-0687. E-mail: avarki@ucsd.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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