摘要
Five new-type Fc receptor molecules were constructed based on streptococcal protein G (SpG) and staphylococcal protein A (SpA). These protein molecules contain one to six Fc binding domains to immunoglobulins which are structurally different from native SpG or SpA. Their expression levels reached 17-30% of the total bacterial proteins after heat induction in E. colt. Immunodiffusion and ELISA results showed that the engineered protein TG (184 amino acid residues) composed of three SpG C3 domain could bind more broadly and efficiently than the native SpG to the IgGs of human, goat, rabbit, etc. , and its optimal pH for binding became wider (pH5-8) compared with the SpG (pH5) ; and the protein TGA (357AA), fused by protein TG and the A, B, C domains of SpA, displayed both the binding pattern of SpG and SpA.
Five new-type Fc receptor molecules were constructed based on streptococcal protein G (SpG) and staphylococcal protein A (SpA). These protein molecules contain one to six Fc binding domains to immunoglobulins which are structurally different from native SpG or SpA. Their expression levels reached 17-30% of the total bacterial proteins after heat induction in E. colt. Immunodiffusion and ELISA results showed that the engineered protein TG (184 amino acid residues) composed of three SpG C3 domain could bind more broadly and efficiently than the native SpG to the IgGs of human, goat, rabbit, etc. , and its optimal pH for binding became wider (pH5-8) compared with the SpG (pH5) ; and the protein TGA (357AA), fused by protein TG and the A, B, C domains of SpA, displayed both the binding pattern of SpG and SpA.
