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.

Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells / S.D. Guglielmetti, I. Tamagnini, D. Mora, M.S. Minuzzo, A. Scarafoni, S. Arioli, J. Hellman, M. Karp, C. Parini. - In: APPLIED AND ENVIRONMENTAL MICROBIOLOGY. - ISSN 0099-2240. - 74:15(2008), pp. 4695-4702. [10.1128/AEM.00124-08]

Implication of an outer surface lipoprotein in adhesion of Bifidobacterium bifidum to Caco-2 cells

S.D. Guglielmetti
Primo
;
D. Mora;M.S. Minuzzo;A. Scarafoni;S. Arioli;C. Parini
Ultimo
2008

Abstract

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.
Settore BIO/10 - Biochimica
Settore AGR/16 - Microbiologia Agraria
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/44939
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