This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dubreuil, J. D.
Right arrow Articles by Rappuoli, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dubreuil, J. D.
Right arrow Articles by Rappuoli, R.

 Previous Article  |  Next Article 

Microbiology and Molecular Biology Reviews, December 2002, p. 617-629, Vol. 66, No. 4
1092-2172/02/$04.00+0     DOI: 10.1128/MMBR.66.4.617-629.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Helicobacter pylori Interactions with Host Serum and Extracellular Matrix Proteins: Potential Role in the Infectious Process

J. Daniel Dubreuil,* Giuseppe Del Giudice, and Rino Rappuoli

IRIS Research Center, Chiron SpA, 53100 Siena, Italy

Helicobacter pylori, a gram-negative spiral-shaped bacterium, specifically colonizes the stomachs of humans. Once established in this harsh ecological niche, it remains there virtually for the entire life of the host. To date, numerous virulence factors responsible for gastric colonization, survival, and tissue damage have been described for this bacterium. Nevertheless, a critical feature of H. pylori is its ability to establish a long-lasting infection. In fact, although good humoral (against many bacterial proteins) and cellular responses are observed, most infected persons are unable to eradicate the infection. A large body of evidence has shown that the interaction between H. pylori and the host is very complex. In addition to the effect of virulence factors on colonization and persistence, binding of specialized bacterial proteins, known as receptins, to certain host molecules (ligands) could explain the success of H. pylori as a chronically persisting pathogen. Some of the reported interactions are of high affinity, as revealed by their calculated dissociation constant. This review examines the binding of host proteins (serum and extracellular matrix proteins) to H. pylori and considers the significance of these interactions in the infectious process. A more thorough understanding of the kinetics of these receptin interactions could provide a new approach to preventing deeper tissue invasion in H. pylori infections and could represent an alternative to antibiotic treatment.

* Corresponding author. Permanent address: Université de Montréal, Faculté de Médecine Vétérinaire, Dép. pathologie et microbiologie, 3200 Sicotte, St-Hyacinthe, Québec, Canada, J2S 7C6. Phone: (450) 773-8521 ext. 8433. Fax: (450) 778-8108. E-mail: daniel.dubreuil{at}umontreal.ca.

Microbiology and Molecular Biology Reviews, December 2002, p. 617-629, Vol. 66, No. 4
1092-2172/02/$04.00+0     DOI: 10.1128/MMBR.66.4.617-629.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Farfan, M. J., Inman, K. G., Nataro, J. P. (2008). The Major Pilin Subunit of the AAF/II Fimbriae from Enteroaggregative Escherichia coli Mediates Binding to Extracellular Matrix Proteins. Infect. Immun. 76: 4378-4384 [Abstract] [Full Text]  
  • Kong, Y., Wu, D., Bai, H., Han, C., Chen, J., Chen, L., Hu, L., Jiang, H., Shen, X. (2008). Enzymatic Characterization and Inhibitor Discovery of a New Cystathionine {gamma}-Synthase from Helicobacter pylori. J Biochem 143: 59-68 [Abstract] [Full Text]  
  • Jenkins, C., Geary, S. J., Gladd, M., Djordjevic, S. P. (2007). The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin. Microbiology 153: 1455-1463 [Abstract] [Full Text]  
  • Jenkins, C., Wilton, J. L., Minion, F. C., Falconer, L., Walker, M. J., Djordjevic, S. P. (2006). Two Domains within the Mycoplasma hyopneumoniae Cilium Adhesin Bind Heparin. Infect. Immun. 74: 481-487 [Abstract] [Full Text]  
  • Dubreuil, J. D., Ruggiero, P., Rappuoli, R., Del Giudice, G. (2004). Effect of heparin binding on Helicobacter pylori resistance to serum. J Med Microbiol 53: 9-12 [Abstract] [Full Text]  
  • Kersulyte, D., Velapatino, B., Mukhopadhyay, A. K., Cahuayme, L., Bussalleu, A., Combe, J., Gilman, R. H., Berg, D. E. (2003). Cluster of Type IV Secretion Genes in Helicobacter pylori's Plasticity Zone. J. Bacteriol. 185: 3764-3772 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»