Previous Article | Next Article ![]()
Applied and Environmental Microbiology, August 2008, p. 4695-4702, Vol. 74, No. 15
0099-2240/08/$08.00+0 doi:10.1128/AEM.00124-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Food Science and Microbiology,1 Department of Biomolecular Sciences and Biotechnology,2 Department of AgriFood Molecular Sciences, University of Milan, Milan, Italy,3 Department of Biochemistry and Food Chemistry/Biotechnology, University of Turku, Turku, Finland,4 Institute of Environmental Engineering and Biotechnology, Tampere University of Technology, Tampere, Finland5
Received 15 January 2008/ Accepted 11 March 2008
We found that the human intestinal isolate Bifidobacterium bifidum MIMBb75 strongly adhered to Caco-2 cells. Proteinase K and lithium chloride treatments showed that proteins play a key role in MIMBb75 adhesion to Caco-2 cells. By studying the cell wall-associated proteins, we identified a surface protein, which we labeled BopA. We purified the protein chromatographically and found that it functioned as an adhesion promoter on Caco-2 cells. In silico analysis of the gene coding for this protein and globomycin experiments showed that BopA is a cysteine-anchored lipoprotein expressed as a precursor polypeptide. A database search indicated that BopA appears to function biologically as an oligopeptide/tripeptide-solute-binding protein in the ABC transport system. We discovered a protein corresponding to BopA and its gene in eight other highly adherent B. bifidum strains. Finally, we found that B. bifidum MIMBb75 and BopA affected the production of interleukin-8 in Caco-2 epithelial cells. BopA is the first protein described to date to be directly involved in the adhesion of bifidobacteria to Caco-2 cells and to show immunomodulatory activity.
Published ahead of print on 6 June 2008.
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»