| 초록 |
Due to high specificity and affinity to target antigen, immunoglobulin G (IgG) antibody has been considered as the most important therapeutic proteins. However, because of glycosylation, most antibody therapeutics have been produced in mammalian hosts and these cause the high cost and poor supply to patients. Even though recent development of aglycosylated antibodies which have effector functions without glycosylation allows the use of E. coli as a host cell for antibody production, still the poor expression and inefficient assembly of IgG in E. coli is remained as a problem to be solved. In this study, we developed the host-vector system for the efficient production of recombinant IgG against anthrax toxin PA. First, several E. coli strains were examined to choose the proper host strain, and different promoters and leader peptides were also examined for the efficient secretion of both heavy and light chains into periplasm of E. coli. Finally co-expression of various factors like asperiplasmic chaperones and foldases were examined to improve the assembly of both chains into full-length IgG in periplasm. |
