Globo-A--a new receptor specificity for attaching Escherichia coli.
Uropathogenic Escherichia coli strains designated as ONAP, based on their O negative A positive agglutination of human P1 erythrocytes, were shown to prefer the globo-A glycolipid as a receptor structure. The dependence on both the A terminal and the globoseries chain was confirmed by agglutination of human AP1, but not Ap or OP1 erythrocytes and by binding to the globo-A glycolipid on TLC plates. Neither Gal alpha 1----4Gal beta nor the A trisaccharide GalNAc alpha 1----3(Fuc alpha 1----2)Gal beta alone functioned as receptors. The bacteria thus appeared to recognize an epitope resulting from the combination of the terminal and internal structures.
D000818:Animals; D001422:Bacterial Adhesion; D001789:Blood Group Antigens; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D004285:Dogs; D004926:Escherichia coli / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D005915:Globosides / Q000097:blood*; D006017:Glycolipids / Q000097:blood*; D006028:Glycosphingolipids / Q000097:blood*; D006384:Hemagglutination; D006801:Humans; D013045:Species Specificity
D001789:Blood Group Antigens; D005915:Globosides; D006017:Glycolipids; D006028:Glycosphingolipids