Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin

Biochemical and Biophysical Research Communications
Hiro-O ItoMasakazu Inoue

Abstract

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.

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Sep 23, 2003·Journal of Microbiological Methods·Hiro O ItoMasakazu Inoue

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Citations

Sep 6, 2006·The Journal of Medical Investigation : JMI·Hiro-O Ito
Jun 1, 2014·Pathogens and Disease·Taihei YamaguchiTakahiko Oho

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