Cloning and expression of Full - length form of Staphylococcal Protein A (SpA) in E. coli

Introduction: Staphylococcal protein A (SpA) plays an important role in the Staphylococcus aureus pathogenesis. The recombinant form of SpA is used extensively in immunology and other biological research. The immobilization of SpA protein onto solid support is frequently used as a consistent and reliable method to purify total IgG from crude protein mixtures that include serum and ascitic fluid. It is also used in the detection of antibodies when coupled with one of the above markers. Method: In this study, a full - length form of SpA was cloned and expressed in Escherichia coli and confirmed by Western blot assay. Results: The results revealed that SpA was expressed and secreted in to medium. For confirmation, Western blot assay was performed using IgG anti goat HRP - conjugated antibodies and the result indicated that the protein was expected one. Conclusions: Expression and Secretion of proteins by E. coli into the growth medium is advantageous over intracellular expression. These benefits include lower production costs, simple downstream processing, and stability of expressed proteins and N - terminal authenticity of the expressed peptide.

E. coli; Expression; Cloning; Full - length SpA