A study on the erythrocyte structures involved in the interaction with mannose-resistant E. coli adhesins.
Research has been carried out on the role of different chemical groups present on human group A erythrocyte membranes and involved in the interaction with mannose-resistant (MR) adhesins of a uropathogenic E. coli strain. For this purpose several enzymes specifically acting on protein, lipid and carbohydrate components have been used to modify the erythrocyte surface structures and the effect produced by these treatments on the agglutinability of red blood cells by E. coli has been studied. Moreover different biological compounds have been tested as possible competitive inhibitors for erythrocyte receptors involved in MR agglutination by E. coli.
D018830:Adhesins, Escherichia coli; D001426:Bacterial Proteins / Q000378:metabolism*; D001798:Blood Proteins / Q000378:metabolism; D004351:Drug Resistance; D004910:Erythrocyte Membrane / Q000378:metabolism / Q000648:ultrastructure*; D004926:Escherichia coli / Q000187:drug effects; D006386:Hemagglutination Tests; D006801:Humans; D008358:Mannose / Q000494:pharmacology*; D010740:Phospholipases / Q000378:metabolism; D002787:Sterol Esterase / Q000378:metabolism
D018830:Adhesins, Escherichia coli; D001426:Bacterial Proteins; D001798:Blood Proteins; D010740:Phospholipases; D002787:Sterol Esterase; D008358:Mannose