@Article{, title={Presentation of Binding-Epitope of Globoseries Glycolipid Receptors is Crucial in the Binding, Colonization and Infection of Escherichia coli}, author={Maan Abul-Milh}, journal={Muthanna Journal of Pure Science (MJPS) مجلة المثنى للعلوم الصرفة}, volume={2}, number={1}, pages={127-152}, year={2014}, abstract={Wild type E. coli DS 17 is a clinical isolate associated withepidemic UTI was studied. This isolate recognized selectivelywell Galα1-4Gal sequence of globoseries glycolipidsseparated on thin-layer chromatogram (TLC), coated inmicrotiter wells and incorporated into liposomes. E.coli DS17,representing a class II adhesin, showed high affinity to thedisaccharide Galα1-4Gal sequence of the globosideglycolipid receptor in all assay systems. Weak recognition ofthe epitope, Galα1-4Gal, in the terminal position ofglobotriaosylceramide (Galα1-4Galβ4Glcβ1Cer) and alsoweak binding of DS17 to the disaccharide sequence withinForssman glycolipid GalNAcα3GalNAcβ3Galα1-4Galβ4Glcβ1Cer. This strain failed to recognize glycolipidsmissing the disaccharide sequence likegangliotetraosylceramide Galβ3GalNAcβ4Galβ4Glcβ1Cer.The modified E. coli DS 17 by replacing class II adhesin withclass III (PrsG) type, (DS17-1), bound Galα1-4Gal sequence ofgloboside less than Forssman glycolipid. E. coli DS17-8strain, DS17 with the knocked out adhesin, revealed nobinding to the glycolipids in all assay system. Usingliposomes aggregation assay, E. coli J96, representing class Iadhesin, showed strong recognition of globosideincorporated into liposomes, weakly when Forssmanglycolipid was used and very weak binding toglobotriaosylceramide was detected.Introduction

} }