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Infection and Immunity, December 1999, p. 6309-6313, Vol. 67, No. 12
Institute of Medical Biochemistry,
Göteborg University, SE 405 30 Göteborg, Sweden
Received 25 June 1999/Returned for modification 22 July
1999/Accepted 23 September 1999
Helicobacter pylori has been shown to agglutinate
erythrocytes in a sialic acid-dependent manner. However, very few
studies have examined relevant target cells in the human stomach.
Neutrophils are required for the onset of gastritis, and the
inflammatory reaction may be induced on contact between bacteria and
neutrophils. In the present work, glycolipids and glycoproteins were
isolated from neutrophils and were studied for binding by overlay with radiolabeled bacteria on thin-layer chromatograms and on membrane blots. There was a complex pattern of binding bands. The
only practical binding activity found was sialic acid dependent,
since treatment of glycoconjugates with neuraminidase or mild
periodate eliminated binding. As shown before for binding to
erythrocytes and other glycoconjugates, bacterial cells grown on agar
bound to many glycoconjugates, while growth in broth resulted in
bacteria that would bind only to polyglycosylceramides, which are
highly heterogeneous and branched
poly-N-acetyllactosamine-containing glycolipids.
Approximately seven positive bands were found for glycoproteins, and
the traditional ganglioside fraction showed a complex, slow-moving
interval with very strong sialic-acid-dependent binding, probably
explained by Fuc substitutions on GlcNAc.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Helicobacter pylori and Neutrophils: Sialic
Acid-Dependent Binding to Various Isolated
Glycoconjugates
*
Corresponding author. Mailing address: Institute of
Medical Biochemistry, Göteborg University, P.O. Box 440, SE 405 30 Göteborg, Sweden. Phone: 46 31 773 3154. Fax: 46 31 41 31 90. E-mail: Halina.Miller-Podraza{at}medkem.gu.se.
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