Infection and Immunity, May 2003, p. 2976-2980, Vol. 71, No. 5
0019-9567/03/$08.00+0 DOI: 10.1128/IAI.71.5.2976-2980.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Susann Teneberg,2 Niamh Roche,2 and Torkel Wadström1*
Department of Medical Microbiology, Dermatology and Infection, Lund University, Lund,1 Institute of Medical Biochemistry, Göteborg University, Göteborg, Sweden2
Received 23 September 2002/ Returned for modification 6 December 2002/ Accepted 17 January 2003
Helicobacter pylori is able to utilize several lectin-like, protein-carbohydrate interactions for binding to mucins, cell surfaces, and extracellular matrix proteins. As determined by hemagglutination assays and binding of radiolabeled bacteria to glycosphingolipids on thin-layer chromatograms, strains of gastric helicobacters and enterohepatic helicobacters, including Helicobacter canis, Helicobacter hepaticus, and Helicobacter bilis, also demonstrated evidence for the presence of lectin-hemagglutinin adhesins. In addition, in H. hepaticus and H. bilis, binding may be sialic acid dependent. The presence or absence and differences in the levels of activity of lectin adhesins may reflect the species' ecological niche.
Present address: Anesthesia Research, Mayo Clinic, Rochester, MN 55905.
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