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Collagen binding of Bifidobacterium adolescentis
1School of Veterinary Medicine and Animal Sciences, Kitasato University, Towada 034, Japan.
Current Microbiology
|May 1, 1997
Summary
Bifidobacterium adolescentis BB-119 specifically adheres to type V collagen through its galactose chains, mediated by two cell surface proteins with lectin-like activity, offering insights into bacterial-host interactions.
Area of Science:
- Microbiology
- Biochemistry
- Cell Biology
Background:
- Extracellular matrix (ECM) proteins play crucial roles in cellular processes.
- Bifidobacteria are important gut commensals with potential health benefits.
- Understanding bacterial adhesion mechanisms is key to harnessing their probiotic potential.
Purpose of the Study:
- To investigate the adherence capabilities of Bifidobacterial strains to various ECM proteins.
- To elucidate the specific molecular interactions between Bifidobacterium adolescentis BB-119 and ECM components.
Main Methods:
- Screening of 13 bifidobacterial strains for ECM protein adhesion.
- Inhibition assays using various collagens, gelatin, and periodate treatment.
- Protease treatment of bacterial cells.
- Ligand blotting with horseradish peroxidase-conjugated type V collagen.
Main Results:
- Two Bifidobacterium adolescentis strains adhered to type I and V collagens.
- B. adolescentis BB-119 adhesion to type V collagen was inhibited by collagens, gelatin, and galactose.
- Protease treatment diminished adhesion, suggesting protein involvement.
- Two cell surface proteins (36 kDa and 52 kDa) from BB-119 bound type V collagen.
Conclusions:
- B. adolescentis BB-119 utilizes specific cell surface proteins to bind type V collagen.
- The adhesion targets galactose chains on type V collagen.
- The interaction involves lectin-like activity of the bacterial surface proteins.