|
Volume 270,
Number 1,
Issue of January 6, 1995 pp. 369-375
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Ligand
Binding by the Immunoglobulin Superfamily Recognition Molecule CD2 Is
Glycosylation-independent
(Received for publication, August 1, 1994; and in revised form, October 3, 1994)
Simon J.
Davis
,
Elizabeth A.
Davies
,
A.
Neil
Barclay
,
Susan
Daenke
,
Dale L.
Bodian
,
E.
Yvonne
Jones
, ,
David
I.
Stuart
, ,
Terry D.
Butters
,
Raymond A.
Dwek
,
P.
Anton
van der Merwe
The evolutionary success of the immunoglobulin superfamily
(IgSF) is thought to reflect the ability of IgSF protein domains to
form stable structural units. The role of glycosylation in stabilizing
these domains is controversial, however. In this study a systematic
analysis of the effect of glycosylation on the ligand-binding
properties of the cell-cell recognition molecule CD2, which consists of
two IgSF domains, was undertaken. A form of human soluble CD2 (hsCD2)
with single N-acetylglucosamine residues at each glycosylation
site was produced by inhibiting glucosidase I with N-butyldeoxynojirimycin during expression in Chinese hamster
ovary cells and digesting the expressed hsCD2 with endoglycosidase H.
The ligand and antibody binding properties of this form of hsCD2 were
indistinguishable from those of fully glycosylated hsCD2 as determined
by surface plasmon resonance analyses. The protein also formed
diffraction quality crystals and analysis of the 2.5-Å resolution
crystal structure indicated that the single N-acetylglucosamine residue present on domain 1 is unlikely to
stabilize the ligand binding face of hsCD2. A second, fully
deglycosylated form of hsCD2 also bound the ligand and antibodies
although this form of the protein tended to aggregate. In contrast to
the results of previous studies, the current data indicate that the
structural integrity and ligand binding function of human CD2 are
glycosylation-independent.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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