HETEROLOGOUS PROTEIN SECRETION AND THE VERSATILE ESCHERICHIA-COLI HEMOLYSIN TRANSLOCATOR

Heterologous proteins synthesized in the Gram-negative bacterium Escherichia coli in bioreactor culture may accumulate in one of three 'compartments': the cytoplasm, the periplasm, or the extracellular medium. Many overexpressed proteins from various origins have been purified from each of these locations. However, to date, each system has required specific tailoring to meet the stringent requirements for each protein product to ensure correct folding, activity and appropriate yield. The E. coli haemolysin secretion system appears to provide a flexible mechanism with which to secrete a wide variety of heterologous fusion proteins into the extracellular medium.