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Glycoconjugate receptors for P-fimbriated Escherichia coli in the mouse. An animal model of urinary tract infection.

Artikel i vetenskaplig tidskrift
Författare B Lanne
B M Olsson
Per-Åke Jovall
Jonas Ångström
H Linder
B I Marklund
Jörgen Bergström
Karl-Anders Karlsson
Publicerad i The Journal of biological chemistry
Volym 270
Nummer/häfte 15
Sidor 9017-25
ISSN 0021-9258
Publiceringsår 1995
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 9017-25
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Animals, Carbohydrate Sequence, Cell Adhesion, Chromatography, High Pressure Liquid, Disease Models, Animal, Escherichia coli, metabolism, Female, Fimbriae, Bacterial, Glycoconjugates, metabolism, Glycolipids, metabolism, Haplorhini, Kidney, metabolism, microbiology, Magnetic Resonance Spectroscopy, Mass Spectrometry, Mice, Mice, Inbred C3H, Models, Molecular, Molecular Sequence Data, Protein Binding, Receptors, Cell Surface, metabolism, Urinary Tract Infections, microbiology
Ämneskategorier Kemi

Sammanfattning

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 Gal alpha 4Gal 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 (Gal alpha 4Gal beta Cer), globotriaosylceramide (Gal alpha 4Gal beta 4Glc beta Cer), globoside (GalNAc beta 3Gal alpha 4Gal beta 4Glc beta Cer), the Forssman glycolipid (GalNAc alpha 3GalNAc beta 3Gal alpha 4Gal beta 4Glc beta Cer), Gal beta 4GlcNAc beta 6(Gal beta 3)GalNAc beta 3Gal alpha 4Gal beta 4Glc beta Cer, and Gal beta 4(Fuc alpha 3)GlcNAc beta 6(Gal beta 3)GalNAc beta 3Gal alpha 4Gal beta 4Glc beta Cer. 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.

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