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Two Variants of Recombinant Human Bone Morphogenetic Protein-2 (rhBMP-2) with Additional Protein Domains: Synthesis in an Escherichia coli Heterologous Expression System

A. S. Karyagina1,2,3, I. S. Boksha1,4, T. M. Grunina1, A. V. Demidenko1, M. S. Poponova1, O. V. Sergienko1,3, A. M. Lyashchuk1, Z. M. Galushkina1, L. A. Soboleva1, E. O. Osidak5, M. S. Bartov1, A. V. Gromov1*, and V. G. Lunin1,3

1Gamaleya Center of Epidemiology and Microbiology, Ministry of Health of the Russian Federation, 123098 Moscow, Russia; E-mail: alexander.v.gromov@gmail.com

2Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia

3Russian Research Institute of Agricultural Biotechnology, 127550 Moscow, Russia

4Mental Health Research Center, 115522 Moscow, Russia

5IMTEK Ltd., 121552 Moscow, Russia

* To whom correspondence should be addressed.

Received August 5, 2016; Revision received December 6, 2016
Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional N-terminal protein domains were obtained by expression in E. coli. The N-terminal domains were s-tag (15-a.a. oligopeptide from bovine pancreatic ribonuclease A) and lz (leucine zipper dimerization domain from yeast transcription factor GCN4). The s-tag-BMP-2 and lz-BMP-2 were purified by a procedure that excluded a long refolding stage. The resulting dimeric proteins displayed higher solubility compared to rhBMP-2 without additional protein domains. Biological activity of both proteins was demonstrated in vitro by induction of alkaline phosphatase in C2C12 cells, and the activity of s-tag-BMP-2 in vivo was shown in various experimental animal models.
KEY WORDS: recombinant bone morphogenetic protein-2, heterologous expression, Escherichia coli

DOI: 10.1134/S0006297917050091