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Journal of Biomedicine and Biotechnology
Volume 2007, Article ID 54327, 6 pages
Research Article

Expression by Streptomyces lividans of the Rat α Integrin CD11b A-Domain as a Secreted and Soluble Recombinant Protein

1Laboratory of Enzymes and Metabolites of Prokaryotes, Center of Biotechnology of Sfax, BP “K”, Sfax 3038, Tunisia
2Molecular Biotechnology Group, Laboratory of Immunology, Institute Pasteur of Tunis, BP 74, Belvédère, Tunis 1002, Tunisia

Received 10 May 2006; Revised 22 September 2006; Accepted 24 October 2006

Academic Editor: Ali Ouaissi

Copyright © 2007 Dorra Zouari Ayadi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


We already reported the use of a long synthetic signal peptide (LSSP) to secrete the Streptomyces sp. TO1 amylase by Streptomyces lividans strain. We herein report the expression and secretion of the rat CD11b A-domain using the same LSSP and S. lividans as host strain. We have used the Escherichia coli/Streptomyces shuttle vector pIJ699 for the cloning of the A-domain DNA sequence downstream of LSSP and under the control of the constitutive ermE-up promoter of Streptomyces erythraeus. Using this construct and S. lividans as a host strain, we achieved the expression of 8 mg/L of soluble secreted recombinant form of the A-domain of the rat leukocyte β2 integrin CD11/CD18 alpha M subunit (CD11b). This secreted recombinant CD11b A-domain reacted with a function blocking antibody showing that this protein is properly folded and probably functional. These data support the capability of Streptomyces to produce heterologous recombinant proteins as soluble secreted form using the “LSSP” synthetic signal peptide.