title: Binding of host-associated treponeme proteins to collagens and laminin: a possible mechanism of spirochetal adherence to host tissues.
abstract: The polypeptides of seven strains of human treponemes were investigated by immunoblot analysis for their binding to the human placental collagens and laminin. Of the treponemal polypeptides, eleven polypeptides, 45-kDa, 49-kDa, and 62-kDa polypeptides from T. pallidum ATCC 27087, a 48-kDa polypeptide from T. phagedenis biotype Reiter, 51-kDa and 53-kDa polypeptides from T. vincentii ATCC 35580, 30-kDa, 53-kDa and 63-kDa polypeptides from T. socranskii subsp. buccale ATCC 35534, a 52-kDa polypeptide from T. denticola ATCC 35405, and a 53-kDa polypeptide from T. denticola ATCC 33520 possessed an ability to bind to the laminin, type I, III, IV, or V collagen. An intermediate-sized human oral isolate strain G7201 did not possess any laminin- or collagen-binding polypeptides. Immunoelectron microscopy using intact treponemal cells with a single collagen-binding polypeptide and the corresponding antisera demonstrated that the 51-kDa and 53-kDa polypeptides from T. vincentii, the 53-kDa polypeptide from T. socranskii subsp. buccale ATCC 35534 and the 52-kDa polypeptide from T. denticola ATCC 35405, were outer envelope proteins.
authors.affiliation: Department of Oral Microbiology, School of Dentistry, Asahi University, Gifu, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Umemoto
authors.forename: I
authors.initials: I
authors.lastname: Namikawa
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D015151:Immunoblotting; D007150:Immunohistochemistry; D007797:Laminin / Q000378:metabolism*; D016253:Microscopy, Immunoelectron; D008970:Molecular Weight; D014208:Treponema / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D007797:Laminin; D003094:Collagen