The pH 6 antigen of Yersinia pestis binds to beta1-linked galactosyl residues in glycosphingolipids

Infect Immun. 1998 Sep;66(9):4545-8. doi: 10.1128/IAI.66.9.4545-4548.1998.


The Yersinia pestis pH 6 antigen was expressed by, and purified from, Escherichia coli containing cloned psa genes. By an enzyme-linked immunosorbence-based assay, purified pH 6 antigen bound to gangliotetraosylceramide (GM1A), gangliotriaosylceramide (GM2A), and lactosylceramide (LC) (designations follow the nomenclature of L. Svennerholm [J. Neurochem. 10:613-623, 1963]). Binding to GM1A, GM2A, and LC was saturable, with 50% maximal binding occurring at 498 +/- 4, 390, and 196 +/- 3 nM, respectively. Thin-layer chromatography (TLC) overlay binding confirmed that purified pH 6 antigen bound to GM1A, GM2A, and LC and also revealed binding to hydroxylated galactosylceramide. Intact E. coli cells which expressed the pH 6 antigen had a specificity similar to that of purified pH 6 in the TLC overlay assay except that nonhydroxylated galactosylceramide was also bound. The binding patterns observed indicate that the presence of beta1-linked galactosyl residues in glycosphingolipids is the minimum determinant required for binding of the pH 6 antigen.

MeSH terms

  • Antigens, Bacterial*
  • Bacterial Proteins / metabolism*
  • Carbohydrate Sequence
  • G(M2) Ganglioside / analogs & derivatives
  • Gangliosides
  • Glycosphingolipids / metabolism*
  • Lactosylceramides / metabolism
  • Molecular Sequence Data
  • Yersinia pestis / metabolism*


  • Antigens, Bacterial
  • Bacterial Proteins
  • G(A1) ganglioside
  • Gangliosides
  • Glycosphingolipids
  • Lactosylceramides
  • pH 6 antigen, Yersinia
  • G(M2) Ganglioside