Recognition of glycoconjugates byHelicobacter pylori: an apparently high-affinity binding of human polyglycosylceramides, a second sialic acid-based specificity

@article{MillerPodraza1996RecognitionOG,
  title={Recognition of glycoconjugates byHelicobacter pylori: an apparently high-affinity binding of human polyglycosylceramides, a second sialic acid-based specificity},
  author={Halina Miller-Podraza and Maan Abul Milh and J{\"o}rgen S. Bergstr{\"o}m and K. -A. Karlsson},
  journal={Glycoconjugate Journal},
  year={1996},
  volume={13},
  pages={453-460}
}
Helicobacter pylori has been reported to agglutinate erythrocytes and to bind to various other cells in a sialic acid-dependent way. The binding was inhibited by sialyllactose or fetuin and other sialylated glycoproteins. The specificity apparently requires bacterial growth on agar, since we found that it was lost after growth in the nutrient mixture Ham's F12. Instead, the bacteria bound with high affinity and in a sialic acid-dependent way to polyglycosylceramides of human erythrocytes, a… CONTINUE READING

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