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.
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This work was supported by Genencor International, Palo Alto, Calif., and the Miami University Office for the Advancement of Scholarship and Teaching.
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Wehner, M.R., Koch, S.R., Kindinger, L. et al. Asparaginase inhibition of adhesion of type 1-fimbriated and P-fimbriated Escherichia coli to epithelial cell receptors. Appl Microbiol Biotechnol 66, 71–73 (2004). https://doi.org/10.1007/s00253-004-1710-7
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DOI: https://doi.org/10.1007/s00253-004-1710-7