title: Collagen binding of Bifidobacterium adolescentis.
abstract: In this study, 13 bifidobacterial strains were tested for their ability to adhere to immobilized extracellular matrix (ECM) proteins. Only two Bifidobacterium adolescentis strains adhered to immobilized type I and type V collagens, but not to laminin, fibronectin, and type III and IV collagens. The adhesion of B. adolescentis BB-119 to type V collagen was inhibited by type I and V collagens and gelatin, and was diminished after protease treatment of the cells. Periodate treatment of immobilized collagen and the presence of galactose inhibited the adhesion of strain BB-119 to type V collagen. Two cell surface proteins with molecular masses of 36 kDa and 52 kDa from strain BB-119 were found to bind to horseradish peroxidase-conjugated type V collagen by ligand blotting. We concluded that B. adolescentis BB-119 binds to type V collagen at galactose chains as target via these two cell surface proteins by their lectin-like activity.
authors.affiliation: School of Veterinary Medicine and Animal Sciences, Kitasato University, Towada 034, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Mukai
authors.forename: T
authors.initials: T
authors.lastname: Toba
authors.forename: H
authors.initials: H
authors.lastname: Ohori
mesh_terms: D001422:Bacterial Adhesion; D001644:Bifidobacterium / Q000378:metabolism*; D001665:Binding Sites; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007422:Intestines / Q000382:microbiology; D011485:Protein Binding
chemical_list: D003094:Collagen