Recognition of glycoconjugates by Helicobacter pylori. Comparison of two sialic acid-dependent specificities based on haemagglutination and binding to human erythrocyte glycoconjugates

Glycoconj J. 1997 Jun;14(4):467-71. doi: 10.1023/a:1018599401772.


Helicobacter pylori expresses separate binding characteristics depending on growth conditions, as documented by binding to human erythrocyte glycoconjugates. Cells grown in Ham's F12 liquid medium exhibited a selective sialic acid-dependent binding to polyglycosylceramides, PGCs (Miller-Podraza et al.(1996) Glycoconjugate J13:453-60). There was no binding to traditional sialylated glycoconjugates like shorter-chain gangliosides, glycophorin or fetuin. However, cells grown on Brucella agar bound both to PGCs and other sialylated glycoconjugates. Fetuin was an effective inhibitor of haemagglutination caused by agar-grown cells, but had no or a very weak inhibitory effect on haemagglutination by F12-grown bacteria. PGCs were strong inhibitors in both cases, while asialofetuin was completely ineffective. The results indicate that H. pylori is able to express two separate sialic acid-dependent specificities, one represented by binding to fetuin, as described before, and another represented by a selective binding to PGCs.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Adhesion*
  • Binding Sites
  • Erythrocytes / metabolism*
  • Glycoconjugates / blood*
  • Helicobacter pylori / physiology*
  • Hemagglutination Tests
  • Humans
  • N-Acetylneuraminic Acid / metabolism*
  • Protein Binding


  • Glycoconjugates
  • N-Acetylneuraminic Acid