Soluble expression of human glycoprotein Ib alpha in Escherichia coli through replacement of the N-terminal capping domain

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Glycoprotein Ib alpha (GpIb alpha), a family of LRR (leucine-rich repeat) proteins, is a membrane protein on the platelet, and plays an important role in atherothrombotic events. The complex formation of GpIb alpha with the von Willebrand Factor (vWF) has been revealed to lead to acute coronary syndrome (ACS) or stroke. A considerable attention has been paid to understand the biological functions of GpIb alpha and its regulation. However, difficulty with the soluble expression of human GpIb alpha in bacteria has hampered the relevant research. Herein, we present a soluble expression of GpIb alpha in Escherichia coli by replacing the N-terminal capping domain of GpIb alpha with that of Internalin B using a computational approach. The resulting protein was expressed as a soluble form in E. coil, maintaining its structural feature and binding property for vWF. The present approach can be broadly used for the soluble expression of human LRR proteins in E. coil.
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Issue Date
2014-09
Language
English
Article Type
Article
Keywords

LEUCINE-RICH REPEAT; VARIABLE LYMPHOCYTE RECEPTORS; VON-WILLEBRAND-FACTOR; VONWILLEBRAND DISEASE; MONOCLONAL-ANTIBODY; PLATELET-ADHESION; PROTEINS; MUTATION

Citation

PROTEIN EXPRESSION AND PURIFICATION, v.101, pp.21 - 27

ISSN
1046-5928
DOI
10.1013/j.pep.2014.06.001
URI
http://hdl.handle.net/10203/193148
Appears in Collection
BiS-Journal Papers(저널논문)BS-Journal Papers(저널논문)
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