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Blood, Vol. 95 No. 1 (January 1), 2000:
pp. 205-211
Threonine-145/Methionine-145 variants of baculovirus
produced recombinant ligand binding domain of GPIb express HPA-2
epitopes and show equal binding of von Willebrand factor
Chester Q. Li,
Stephen F. Garner,
Julian Davies,
Peter A. Smethurst,
Mark R. Wardell, and
Willem H. Ouwehand
From the Department of Hematology, University of Cambridge, National
Blood Service East Anglia, Cambridge, UK; National Institute for
Biological Standards and Control, Potters Bar, UK; and the Department
of Biochemistry and Molecular Biophysics, Washington University School
of Medicine, St. Louis, MO.
Glycoprotein (GP) Ib is the functionally dominant subunit
of the platelet GPIb-IX-V receptor complex, with the von
Willebrand factor (vWF) binding site residing on the
amino-terminus. A threonine for methionine-145 replacement of GPIb
is associated with the human platelet antigen (HPA)-2
system. To study the structural and functional consequences of this
mutation, both forms of GPIb were expressed as calmodulin fusion
proteins in insect cells. Both recombinant proteins were
recognized by their respective alloantibodies, independent of
glycosylation or intactness of disulfide bonds, and gave similar
results to platelet-derived GPIb in antibody detection assays.
Resonant mirror studies showed that vWF binding was not affected by the
HPA-2 mutation; however, vWF binding was partially inhibited by IgG
HPA-2 antibodies. Our data are compatible with an involvement of the
leucine-rich repeat domain of GPIb in vWF binding and
indicate that recombinant GPIb may be used to detect HPA-2
antibodies. (Blood. 2000;95:205-211)
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