The pH 6 Antigen of Yersinia pestisBinds to β1-Linked Galactosyl Residues in Glycosphingolipids

Dean Payne, David Tatham, E. Diane Williamson, Richard W. Titball, J. T. Barbieri
1998 Infection and Immunity  
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,
more » ... ly. 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 ␤1-linked galactosyl residues in glycosphingolipids is the minimum determinant required for binding of the pH 6 antigen.
doi:10.1128/iai.66.9.4545-4548.1998 fatcat:rgvwj5cforeihbak4fjo6nv3xu