Globo-A--a new receptor specificity for attaching Escherichia coli

FEBS Lett. 1988 Sep 12;237(1-2):123-7. doi: 10.1016/0014-5793(88)80184-4.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Adhesion*
  • Blood Group Antigens*
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Dogs
  • Escherichia coli / genetics
  • Escherichia coli / isolation & purification
  • Escherichia coli / physiology*
  • Globosides / blood*
  • Glycolipids / blood*
  • Glycosphingolipids / blood*
  • Hemagglutination*
  • Humans
  • Species Specificity


  • Blood Group Antigens
  • Globosides
  • Glycolipids
  • Glycosphingolipids