Role of Extracellular Transaldolase from Bifidobacterium bifidum in Mucin Adhesion and Aggregation
0301 basic medicine
570
Probiotics
Cell Membrane
Mucins
Membrane Proteins
Epithelial Cells
Bacterial Adhesion
Transaldolase
Intestines
03 medical and health sciences
Humans
Bifidobacterium
HT29 Cells
DOI:
10.1128/aem.08024-11
Publication Date:
2012-03-24T07:34:07Z
AUTHORS (8)
ABSTRACT
ABSTRACT
The ability of bifidobacteria to establish in the intestine of mammals is among the main factors considered to be important for achieving probiotic effects. The role of surface molecules from
Bifidobacterium bifidum
taxon in mucin adhesion capability and the aggregation phenotype of this bacterial species was analyzed. Adhesion to the human intestinal cell line HT29 was determined for a collection of 12
B. bifidum
strains. In four of them—
B. bifidum
LMG13195, DSM20456, DSM20239, and A8—the involvement of surface-exposed macromolecules in the aggregation phenomenon was determined. The aggregation of
B. bifidum
A8 and DSM20456 was abolished after treatment with proteinase K, this effect being more pronounced for the strain A8. Furthermore, a mucin binding assay of
B. bifidum
A8 surface proteins showed a high adhesive capability for its transaldolase (Tal). The localization of this enzyme on the surface of
B. bifidum
A8 was unequivocally demonstrated by immunogold electron microscopy experiments. The gene encoding Tal from
B. bifidum
A8 was expressed in
Lactococcus lactis
, and the protein was purified to homogeneity. The pure protein was able to restore the autoaggregation phenotype of proteinase K-treated
B. bifidum
A8 cells. A recombinant
L. lactis
strain, engineered to secrete Tal, displayed a mucin- binding level more than three times higher than the strain not producing the transaldolase. These findings suggest that Tal, when exposed on the cell surface of
B. bifidum
, could act as an important colonization factor favoring its establishment in the gut.
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