Glycoconjugate Receptors for P-fimbriated Escherichia coli in the Mouse AN ANIMAL MODEL OF URINARY TRACT INFECTION

Abstract Glycosphingolipids were isolated from kidneys, urethers, and bladders (including urethrae) of C3H/HeN mice. Binding was studied of a clinical isolate and recombinant strains of uropathogenic P-fimbriated Escherichia coli to these glycolipids. A series of receptor-active glycolipids with Galα4Gal in common, previously shown to be recognized by these bacteria, was identified by use of specific monoclonal antibodies, fast-atom bombardment and electron-impact mass spectrometry, and proton nuclear magnetic resonance spectroscopy: galabiosylceramide (Galα4GalβCer), globotriaosylceramide (Galα4Galβ4GlcβCer), globoside (GalNAcβ3Galα4Galβ4GlcβCer), the Forssman glycolipid (GalNAcα3GalNAcβ3Galα4Galβ4GlcβCer), Galβ4GlcNAcβ6(Galβ3)GalNAcβ3Galα4Galβ4GlcβCer, and Galβ4(Fucα3)GlcNAcβ6(Galβ3)GalNAcβ3Galα4Galβ4GlcβCer. The binding pattern for mouse kidney glycolipids differed from that for kidney glycolipids of man and monkey. In particular, the dominant 8-sugar glycolipid in the mouse was not detected in the primates. A second difference was found in the binding of E. coli to kidney glycoproteins on blots after electrophoresis; the mouse showed distinct receptor-active bands while human and monkey did not. These differences may be of relevance when using the mouse as a model for clinical urinary tract infection of man.