title: Recognition of glycoconjugates by Helicobacter pylori. Comparison of two sialic acid-dependent specificities based on haemagglutination and binding to human erythrocyte glycoconjugates.
abstract: 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.
authors.affiliation: Department of Medical Biochemistry, Göteborg University, Sweden.
authors.forename: H
authors.initials: H
authors.lastname: Miller-Podraza
authors.forename: J
authors.initials: J
authors.lastname: Bergström
authors.forename: M A
authors.initials: MA
authors.lastname: Milh
authors.forename: K A
authors.initials: KA
authors.lastname: Karlsson
mesh_terms: 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
chemical_list: D006001:Glycoconjugates; D019158:N-Acetylneuraminic Acid