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

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.

journal_name

Appl Environ Microbiol

authors

Guglielmetti S,Tamagnini I,Mora D,Minuzzo M,Scarafoni A,Arioli S,Hellman J,Karp M,Parini C

doi

10.1128/AEM.00124-08

subject

Has Abstract

pub_date

2008-08-01 00:00:00

pages

4695-702

issue

15

eissn

0099-2240

issn

1098-5336

pii

AEM.00124-08

journal_volume

74

pub_type

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