African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12496

Full Length Research Paper

Expression of recombinant Streptokinase from local Egyptian Streptococcus sp. SalMarEg

Sobhy Al Sohaimy1, Eiman Aleem3*, Elsayed E Hafez2, Sally S Esmail1, Muhammad El-Saadani4 and Nihad Abdel Moneim4
1Department of Agricultural Industries and Food Technology, 2Plant Molecular Pathology Department, Arid Lands Cultivation and Development Research Institute (ALCDRI), City of Scientific Research and Technology Applications (CSAT), Universities and Research Centers District, New Borg Elarab, 21934, Alexandria, Egypt. 3Division of Molecular Biology, Zoology Department, 4Biochemistry Department, Faculty of Science, Alexandria University, Moharam Bey 21511, Alexandria, Egypt.
Email: [email protected]

  •  Accepted: 13 May 2011
  •  Published: 17 August 2011

Abstract

Streptokinase (SK) is a therapeutically important thrombolytic agent. Cardiovascular disease is the first cause of adult death worldwide. In Egypt about 13% of the population die every year due to ischemic heart disease. In spite of this fact, there is no local production of cardiovascular therapeutics. We reported for the first time the expression of a recombinant SK from a local Streptococcus strain. When produced on industrial scale this r-SK may substantially contribute to reducing the costs of thrombolytic therapy in developing countries. In this study, a highly purified r-SK from Streptococcus sp. isolated from Egyptian pharyngitis patients was obtained. The isolated strain was partially identified using 16S rDNA sequencing and namedStreptococcus sp. SalMarEg. It was found to be phylogenetically related toStreptococcus pyogenes. Analysis of the obtained sequence showed high similarity with other SK genes. The protein expression in a prokaryotic system obtained a 47-kDa SK protein that could be purified using a single-step his-tagged affinity purification chromatography, with nearly 80% recovery. The clot lytic activities of both recombinant and commercial SK were similar, thus giving the basis to scale up this SK product in order to evaluate the possibilities of its commercialization in local and/or regional markets.

 

Key words: Streptokinase, Streptococcus SalMarEg, thrombolytic agent,heterologous expression.

Abbreviation

SK, Streptokinase; r, recombinant.