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 A or OP₁, erythrocytes and by binding to the globo-A glycolipid on TLC plates. Neither Galαl→Ga1β nor the A trisaccharide GalNAcαl→ 3(Fucαl→2)Galβ alone functioned as receptors. The bacteria thus appeared to recognize an epitope resulting from the combination of the terminal and internal structures.