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Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor
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| Zeitschriftentitel: | Blood |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Blood, 95, 2000, 1, S. 205-211 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society of Hematology
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| Schlagwörter: |
| author_facet |
Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. |
|---|---|
| author |
Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. |
| spellingShingle |
Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. Blood Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor Cell Biology Hematology Immunology Biochemistry |
| author_sort |
li, chester q. |
| spelling |
Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. 1528-0020 0006-4971 American Society of Hematology Cell Biology Hematology Immunology Biochemistry http://dx.doi.org/10.1182/blood.v95.1.205 <jats:title>Abstract</jats:title><jats:p>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)</jats:p> Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor Blood |
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Biologie Medizin Chemie und Pharmazie |
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American Society of Hematology, 2000 |
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American Society of Hematology, 2000 |
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1528-0020 0006-4971 |
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2000 |
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49 |
| title |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_unstemmed |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_full |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_fullStr |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_full_unstemmed |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_short |
Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_sort |
threonine-145/methionine-145 variants of baculovirus produced recombinant ligand binding domain of gpibα express hpa-2 epitopes and show equal binding of von willebrand factor |
| topic |
Cell Biology Hematology Immunology Biochemistry |
| url |
http://dx.doi.org/10.1182/blood.v95.1.205 |
| publishDate |
2000 |
| physical |
205-211 |
| description |
<jats:title>Abstract</jats:title><jats:p>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)</jats:p> |
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| author | Li, Chester Q., Garner, Stephen F., Davies, Julian, Smethurst, Peter A., Wardell, Mark R., Ouwehand, Willem H. |
| author_facet | Li, Chester Q., Garner, Stephen F., Davies, Julian, Smethurst, Peter A., Wardell, Mark R., Ouwehand, Willem H., Li, Chester Q., Garner, Stephen F., Davies, Julian, Smethurst, Peter A., Wardell, Mark R., Ouwehand, Willem H. |
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| description | <jats:title>Abstract</jats:title><jats:p>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)</jats:p> |
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| imprint | American Society of Hematology, 2000 |
| imprint_str_mv | American Society of Hematology, 2000 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 205-211 |
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| spelling | Li, Chester Q. Garner, Stephen F. Davies, Julian Smethurst, Peter A. Wardell, Mark R. Ouwehand, Willem H. 1528-0020 0006-4971 American Society of Hematology Cell Biology Hematology Immunology Biochemistry http://dx.doi.org/10.1182/blood.v95.1.205 <jats:title>Abstract</jats:title><jats:p>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)</jats:p> Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor Blood |
| spellingShingle | Li, Chester Q., Garner, Stephen F., Davies, Julian, Smethurst, Peter A., Wardell, Mark R., Ouwehand, Willem H., Blood, Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor, Cell Biology, Hematology, Immunology, Biochemistry |
| title | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_full | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_fullStr | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_full_unstemmed | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_short | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| title_sort | threonine-145/methionine-145 variants of baculovirus produced recombinant ligand binding domain of gpibα express hpa-2 epitopes and show equal binding of von willebrand factor |
| title_unstemmed | Threonine-145/Methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbα express HPA-2 epitopes and show equal binding of von Willebrand factor |
| topic | Cell Biology, Hematology, Immunology, Biochemistry |
| url | http://dx.doi.org/10.1182/blood.v95.1.205 |