Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin.
To characterize fibronectin binding with Granulicatella adiacens, a causative agent of infective endocarditis, monoclonal antibodies were generated against human fibronectin and selected for their capacity to inhibit the fibronectin binding of the organism. Thermolysin and lysyl-endopeptidase digests of fibronectin were characterized by Western blot. The epitope of inhibitory monoclonal antibody was found in the central portion of fibronectin known as the cell-binding domain, and not in the N-terminal portion known to be the binding region of most microbial species, e.g., Staphylococcus aureus and Streptococcus pyogenes. While these two species could bind to both the N-terminal and central portion, Escherichia coli and G. adiacens bind only to the latter. Excess amounts of free fibronectin in the solution inhibited the bacterial adherence to the N-terminal fibronectin fragment, but not to the central region, thereby suggesting the central region plays a significant role for in vivo bacterial colonization in the presence of high concentrations of soluble fibronectin.
Ito
Hiro-O
HO
Department of Preventive Dentistry, Kagoshima University Graduate School of Medical and Dental Sciences, Kagoshima 890-8544, Japan. dearkids@dentb.hal.kagoshima-u.ac.jp
Soutome
Sakiko
S
Nokihara
Kiyoshi
K
Inoue
Masakazu
M
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry / Q000276:immunology; D018604:Epitope Mapping; D005260:Female; D005353:Fibronectins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007777:Lactobacillaceae / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D020449:Repetitive Sequences, Amino Acid
D000911:Antibodies, Monoclonal; D005353:Fibronectins