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

@article{Payne1998TheP6,
  title={The pH 6 antigen of Yersinia pestis binds to beta1-linked galactosyl residues in glycosphingolipids.},
  author={Dean W. Payne and Daniel John Tatham and E D Williamson and Richard W. Titball},
  journal={Infection and immunity},
  year={1998},
  volume={66 9},
  pages={
          4545-8
        }
}
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… CONTINUE READING

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 35 CITATIONS

Attachment of Yersinia pestis to human respiratory cell lines is inhibited by certain oligosaccharides.

  • Journal of medical microbiology
  • 2006
VIEW 8 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED