Charlotte Jeanneau and Maram Morjen have equally contributed to this work.
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Cell Culture and Tissue Engineering
Expression of a functional recombinant C-type lectin-like protein lebecetin in the human embryonic kidney cells
Article first published online: 19 OCT 2012
DOI: 10.1002/btpr.1632
Copyright © 2012 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Jebali, J., Jeanneau, C., Morjen, M., Mathieu, S., Bazaa, A., el Ayeb, M., Luis, J., Gargouri, A., Marrakchi, N. and el Battari, A. (2012), Expression of a functional recombinant C-type lectin-like protein lebecetin in the human embryonic kidney cells. Biotechnol Progress, 28: 1560–1565. doi: 10.1002/btpr.1632
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Charlotte Jeanneau and Maram Morjen have equally contributed to this work.
Publication History
- Issue published online: 4 DEC 2012
- Article first published online: 19 OCT 2012
- Accepted manuscript online: 7 SEP 2012 08:20AM EST
- Manuscript Revised: 14 AUG 2012
- Manuscript Received: 9 JUL 2012
- Abstract
- Article
- References
- Cited By
Keywords:
- snake venom;
- lebecetin;
- C-type lectin;
- heterodimerization;
- integrin
Abstract
Lebecetin is an anticoagulant C-type lectin-like protein that was previously isolated from Macrovipera lebetina venom and described to consist of two subunits (alpha and beta). It was reported to potently prevent platelet aggregation by binding to glycoprotein Ib and to exhibit a broad spectrum of inhibitory activities on various integrin-mediated functions of tumor cells, including adhesion, proliferation, and cell migration. This study aimed to investigate the structure-function of lebecetin. Accordingly, the cDNA of each subunit was cloned and separately or jointly expressed in the human embryonic kidney cells using two vectors with different selectable tags. The immunofluorescence analysis of transfected cells revealed significant expression levels and co-localization of the two lebecetin subunits. The recombinant proteins were efficiently secreted and purified using metal-chelating affinity chromatography. We found that the Lebecetin alpha and beta subunits were produced as a mixture of homodimers and heterodimers and that the heterodimerization represents a prerequisite for functioning. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012