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

Abstract

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.