Proteolytic degradation of Human Tamm-Horsfall Protein by protease from pathogenic Escherichia coli and selection for attenuated mutant.

Abstract

A protease was successfully purified from the Uropathogenic Escherichia coli (UPEC). The optimum temperature and pH of protease was 40 °C and pH 7 respectively. Pre-incubation at temperatures above 50C resulted in a decrease of enzyme activity, indicating that protease A is a thermally unstable enzyme. The optimal pH for protease stability was range from pH 6.5 to 7.5 and the enzyme activity was stable over a broad range of temperature 15-50 °C, through which it retained at least 80% of its original activity. Uropathogenic Escherichia coli (UPEC) is a causative agent in the vast majority of urinary tract infections (UTIs), such as bladder infection ( cystitis) , (Kidney infection) pyelonephritis, and other infectious complications, which may result in acute renal failure in healthy individuals as well as in renal transplant patients. In this repory  we focused on  Human Tamm-Horsfall glycoprotein, the major urinary protein, is a glycosyl-phosphatidyl-inositol (GPI)   has a high gel-forming tendency, it has been postulated that it takes part in the water impermeability of TAL. It is also proposed that the Tamm-Horsfall protein plays a protective role towards pyelonephritogenic pathogens such as Escherichia coli. The Tamm-Horsfall protein may inhibit the colonization of these pathogens in the renal mucosa in that the soluble form competes with that exposed at the plasma membrane.