Recognition of glycoconjugates by Helicobacter pylori. Comparison of two sialic acid-dependent specificities based on haemagglutination and binding to human erythrocyte glycoconjugates.
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.
Miller-Podraza
H
H
Department of Medical Biochemistry, Göteborg University, Sweden.
Bergström
J
J
Milh
M A
MA
Karlsson
K A
KA
D001422:Bacterial Adhesion; D001665:Binding Sites; D004912:Erythrocytes / Q000378:metabolism*; D006001:Glycoconjugates / Q000097:blood*; D016480:Helicobacter pylori / Q000502:physiology*; D006386:Hemagglutination Tests; D006801:Humans; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D011485:Protein Binding
D006001:Glycoconjugates; D019158:N-Acetylneuraminic Acid