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

Artikel i vetenskaplig tidskrift
Författare Halina Miller-Podraza
Maan Abul Milh
Jörgen Bergström
Karl-Anders Karlsson
Publicerad i Glycoconjugate journal
Volym 13
Nummer/häfte 3
Sidor 453-60
ISSN 0282-0080
Publiceringsår 1996
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 453-60
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Binding Sites, Carbohydrate Sequence, Chromatography, Thin Layer, Erythrocyte Membrane, chemistry, Glycoconjugates, analysis, Glycolipids, analysis, Glycosphingolipids, blood, isolation & purification, Helicobacter pylori, chemistry, cytology, growth & development, Humans, Lactose, analogs & derivatives, Membrane Glycoproteins, blood, Molecular Sequence Data, N-Acetylneuraminic Acid, Sensitivity and Specificity, Sialic Acids, alpha-Fetoproteins
Ämneskategorier Kemi

Sammanfattning

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 still incompletely characterized group of complex glycolipids. Bacteria grown in F12 medium were metabolically labelled with 35S-methionine and analysed for binding to glycolipids on thin-layer chromatograms and to glycoproteins on blots after electrophoresis, with human erythrocyte glycoconjugates in focus. There was no binding to simpler gangliosides including GM3 or sialylparagloboside, or to a mixture of brain gangliosides. In contrast, polyglycosylceramides of human erythrocyte membranes bound at a pmol level. The activity was eliminated by mild acid treatment, mild periodate oxidation or sialidase hydrolysis. Erythrocyte proteins as well as a range of reference glycoproteins did not bind except band 3, which was weakly active. However, this activity was resistant to periodate oxidation. These results indicate a second and novel sialic acid-recognizing specificity which is expressed independently of the previously described specificity.

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