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Infection and Immunity, September 1998, p. 4545-4548, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The pH 6 Antigen of Yersinia pestis Binds to beta 1-Linked Galactosyl Residues in Glycosphingolipids

Dean Payne, David Tatham, E. Diane Williamson, and Richard W. Titball*

Defence Evaluation and Research Agency, CBD Porton Down, Porton Down, Salisbury, Wiltshire SP4 OJQ, United Kingdom

Received 13 April 1998/Returned for modification 15 May 1998/Accepted 11 June 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 beta 1-linked galactosyl residues in glycosphingolipids is the minimum determinant required for binding of the pH 6 antigen.

* Corresponding author. Mailing address: Defence Evaluation and Research Agency, CBD Porton Down, Porton Down, Salisbury, Wiltshire SP4 OJQ, United Kingdom. Phone: 1980 613103. Fax: 0980 613284. E-mail: 100655,2360{at}compuserve.com.

Infection and Immunity, September 1998, p. 4545-4548, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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