This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Roche, N. Articles by Teneberg, S. Search for Related Content PubMed PubMed Citation Articles by Roche, N. Articles by Teneberg, S.

 Previous Article  |  Next Article 

Infection and Immunity, March 2004, p. 1519-1529, Vol. 72, No. 3
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.3.1519-1529.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Helicobacter pylori and Complex Gangliosides

Institute of Medical Biochemistry, Göteborg University, SE 405 30 Göteborg,¹ Department of Odontology/Oral Microbiology, Umeå University, SE 901 87 Umeå, Sweden²

Received 14 July 2003/ Returned for modification 22 October 2003/ Accepted 26 November 2003

Recognition of sialic acid-containing glycoconjugates by the human gastric pathogen Helicobacter pylori has been repeatedly demonstrated. To investigate the structural requirements for H. pylori binding to complex gangliosides, a large number of gangliosides were isolated and characterized by mass spectrometry and proton nuclear magnetic resonance. Ganglioside binding of sialic acid-recognizing H. pylori strains (strains J99 and CCUG 17874) and knockout mutant strains with the sialic acid binding adhesin SabA or the NeuAc3Galß4GlcNAcß3Galß4GlcNAcß-binding neutrophil-activating protein HPNAP deleted was investigated using the thin-layer chromatogram binding assay. The wild-type bacteria bound to N-acetyllactosamine-based gangliosides with terminal 3-linked NeuAc, while gangliosides with terminal NeuGc3, NeuAc6, or NeuAc8NeuAc3 were not recognized. The factors affecting binding affinity were identified as (i) the length of the N-acetyllactosamine carbohydrate chain, (ii) the branches of the carbohydrate chain, and (iii) fucose substitution of the N-acetyllactosamine core chain. While the J99/NAP^- mutant strain displayed a ganglioside binding pattern identical to that of the parent J99 wild-type strain, no ganglioside binding was obtained with the J99/SabA^- mutant strain, demonstrating that the SabA adhesin is the sole factor responsible for the binding of H. pylori bacterial cells to gangliosides.

Editor: J. N. Weiser

This article has been cited by other articles:

• Goodwin, A. C., Weinberger, D. M., Ford, C. B., Nelson, J. C., Snider, J. D., Hall, J. D., Paules, C. I., Peek, R. M. Jr, Forsyth, M. H. (2008). Expression of the Helicobacter pylori adhesin SabA is controlled via phase variation and the ArsRS signal transduction system. Microbiology 154: 2231-2240 [Abstract] [Full Text]  
• Kusters, J. G., van Vliet, A. H. M., Kuipers, E. J. (2006). Pathogenesis of Helicobacter pylori Infection. Clin. Microbiol. Rev. 19: 449-490 [Abstract] [Full Text]  
• Yamaoka, Y, Ojo, O, Fujimoto, S, Odenbreit, S, Haas, R, Gutierrez, O, El-Zimaity, H M T, Reddy, R, Arnqvist, A, Graham, D Y (2006). Helicobacter pylori outer membrane proteins and gastroduodenal disease. Gut 55: 775-781 [Abstract] [Full Text]  
• Unemo, M., Aspholm-Hurtig, M., Ilver, D., Bergstrom, J., Boren, T., Danielsson, D., Teneberg, S. (2005). The Sialic Acid Binding SabA Adhesin of Helicobacter pylori Is Essential for Nonopsonic Activation of Human Neutrophils. J. Biol. Chem. 280: 15390-15397 [Abstract] [Full Text]