Asparaginase inhibition of adhesion of type 1-fimbriated and P-fimbriated Escherichia coli to epithelial cell receptors.

ABSTRACT

The 3D structures of Fim H and PapG proteins complexed with the host carbohydrate receptor demonstrate that both utilize binding-pocket asparagines for contact or stabilization with the carbohydrate. Pretreatment of whole bacteria with asparaginase resulted in decreased fimbriae-mediated attachment to urinary epithelial cells. Enzyme treatment of bacteria pre-adhered to epithelial cells removed more uropathogenic E. coli than the indigenous flora attached to them.