Specificity of binding of a strain of uropathogenic Escherichia coli to Gal alpha 1—-4Gal-containing glycosphingolipids.

作者：Klaus Bock, Michael E. Breimer, A Brignole, Gunnar C. Hansson, K.‐A. Karlsson, Göran Larson, Hakon Leffler, Bo E. Samuelsson, Nicklas Strömberg, C S Edén · 发表于：Journal of Biological Chemistry · 年份：1985 · DOI：10.1016/s0021-9258(17)39507-8 · 被引用次数：294 · 研究领域：Glycosylation and Glycoproteins Research、Erythrocyte Function and Pathophysiology、Lipid Membrane Structure and Behavior

A strain of Escherichia coli originally isolated from urine of a patient with acute pyelonephritis was studied in detail for binding to glycosphingolipids. Bacteria labeled metabolically with [14C]glucose were layered over a glycolipid chromatogram and bound bacteria were detected by autoradiography. The detection was down to a few ng of glycolipid (pmol level) under these assay conditions. At a test level of 500 ng all glycolipids (more than a dozen molecular species analyzed) with Gal alpha 1----4Gal as an internal or terminal part bound the bacteria strongly while glycolipids known to lack this sequence were negative. Conformational analysis using hard sphere calculations including the exo-anomeric effect showed a bend in the saccharide chain at this disaccharide with a largely hydrophobic surface of the convex side, probably being part of the binding epitope. Mixtures of glycolipids isolated from a human ureter scraping and from urinary sediments bound bacteria in the 2- to 7-sugar interval. Thus, this infectious strain of E. coli recognizes glycolipids being present in epithelial cells lining the urinary tract.