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Volume 272, Number 30, Issue of July 25, 1997 pp. 19067-19071
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Carbohydrate Binding Specificity of the Neutrophil-activating Protein of Helicobacter pylori

(Received for publication, May 5, 1997)

Susann Teneberg Dagger , Halina Miller-Podraza Dagger , Heather C. Lampert , Doyle J. Evans Jr. , Dolores G. Evans , Dan Danielsson par and Karl-Anders Karlsson Dagger

From the Dagger  Department of Medical Biochemistry, Göteborg University, Medicinaregatan 9A, S-413 90 Göteborg, Sweden, the  Bacterial Enteropathogens Laboratory, Veterans Affairs Medical Center and Baylor College of Medicine, Houston, Texas 77030, and the par  Department of Clinical Microbiology and Immunology, Örebro Medical Center, S-701 85 Örebro, Sweden

The possible interaction of the neutrophil-activating protein of Helicobacter pylori with target cell glycoconjugates was investigated by the binding of 125I-labeled recombinant protein to glycosphingolipids from human neutrophils in solid phase assays. Thereby, a distinct binding of the neutrophil-activating protein to four bands in the acid glycosphingolipid fraction from human neutrophils was detected, whereas no binding to the non-acid glycosphingolipids or polyglycosyl ceramides from these cells was obtained. When using glycosphingolipids not present in the cell membrane of human neutrophils, it was found that the neutrophil-activating protein also bound to sulfated glycosphingolipids as sulfatide and sulfated gangliotetraosyl ceramide. Comparison of the binding preferences of the protein to reference glycosphingolipids from other sources suggested that in human granulocytes, the neutrophil-activating protein of H. pylori preferentially recognizes glycoconjugates with a terminally unsubstituted NeuAcalpha 3Galbeta 4GlcNAcbeta 3Galbeta 4GlcNAcbeta sequence.


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