The binding of Proteus mirabilis nonagglutinating fimbriae to ganglio-series asialoglycolipids and lactosyl ceramide.

Proteus mirabilis is a common opportunistic Gram-negative uropathogen that infects the upper urinary tract. We have examined the role of the nonagglutinating fimbriae (NAF) of P. mirabilis in mediating bacterial adhesion to cell surface receptors. Purified NAF of P. mirabilis were demonstrated to bind to a number of glycolipids, including asialo-GM1, asialo-GM2, and lactosyl ceramide (LacCer) in solid-phase binding assays and in thin layer chromatography (TLC) overlay assays. Furthermore, preincubation of the biotinylated NAF (Bt-NAF) with anti-NAF monoclonal antibodies resulted in inhibition of NAF binding to immobilized asialo-GM1, asialo-GM2, and LacCer. In adherence assays, P. mirabilis binding to Madin-Darby canine kidney (MDCK) cells was inhibited by murine anti-asialo-GM1 monoclonal antibodies H2G10 to about 50% of the binding level in the absence of the antibody, specific for the terminal beta-galactopyranosyl residue of asialo-GM1 (Harrison et al. 1998). The results of this study suggest that NAF of P. mirabilis recognize a GalNAc beta 1-4Gal moiety present in the ganglio-series of asialoglycolipids, and that the terminal beta-galactopyranosyl-containing glycoconjugates play a role in NAF-mediated adherence of P. mirabilis to MDCK cells. Similarly to other bacteria, P. mirabilis NAF was also shown to express the LacCer specificity.