Two kinds of P-fimbrial variants of uropathogenic Escherichia coli recognizing forssman glycosphingolipid.

Various types of fimbriae on pathogenic Escherichia coli strains have been classified by their antigenicities and recognition specificities for receptors. However, the antigenicity of fimbrial proteins does not always correlate with the fimbrial recognition specificity. In this communication, the exact carbohydrate structures recognized by the fimbriae of two human uropathogenic E. coli strains, KS71 (O4) and IH11024 (O6), that have P-fimbrial antigen, were examined. Strain KS71 showed mannose-resistant (MR) hemagglutination (HA) of human blood group OP1 phenotype erythrocytes, and its HA was inhibited by blood group Pk antigen, Gal(alpha,1-4)Gal(beta,1-4)Glc-ceramide and P antigen, GalNAc(beta,1-3)Gal (alpha,1-4)Gal(beta,1-4)Glc-ceramide but not by Forssman antigen, GalNAc(alpha,1-3)GalNAc(beta,1-3)Gal(alpha,1-4)Gal (beta,1-4)Glc-ceramide, as previously described in many papers. The cells also showed MR HA of sheep erythrocytes, which was potently inhibited by Forssman, and weakly by P and Pk antigens. These phenomena could not be explained by the above P adhesin specificity. This adhesin was called Forssman-like adhesin. Strain IH11024 also caused MR HA of sheep erythrocytes but not of human erythrocytes. The HA was inhibited specifically by Forssman but neither by Pk nor P antigen. This adhesin was completely different from P adhesin and Forssman-like adhesin in recognition of the carbohydrate epitope. This adhesin, until now called a pseudotype of P fimbriae, was renamed Forssman adhesin.