[ODP6A] a. Adhesion Factors, and Colonization Factors

[ODP-113] Inhibition of the interaction between fibronectin and dermatopontin by Clostridium perfringens Fbps

○Seira Egusa¹, Nozomu Matsunaga¹, Nodoka Narukawa¹, Tsutomu Yamasaki², Ryousuke Akamatsu¹, Seiichi Katayama¹, Yasuo Hitsumoto¹ (¹Dept. Life Science, Fac. Science, Okayama Univ. of Science, ²Pharmaceutical Department, Shujitsu Univ.)

Fibronectin (Fn), one of the extracellular matrix proteins (ECM), is approximately 450 kDa glycoprotein and consists of 12 type I, 2 type II, and 15–17 type III modules. Fibrillation of Fn is important for tissue reconstitution and wound healing. In our previous reports, it was found that Clostridium perfringens produce several Fn-binding proteins (Fbps).
Dermatopontin (DPT), a 22 kDa non-collagenous extracellular matrix protein, accelerates normal collagen fibrillation and induces Fn fibrillation. DPT binds to Fn-type III_12-14 (III_12-14), leading to change Fn conformation and promote Fn fibrillation. Here, we investigated the effects of two Fbps of them, FbpA and FbpB, on the DPT-induced Fn-fibrillation and the binding of Fn and III_12-14 to DPT. Both recombinant FbpA (rFbpA) and recombinant FbpB (rFbpB) inhibited DPT-induced Fn-fibrillation and significantly inhibited Fn binding to DPT and recombinant III_12-14 (rIII_12-14) binding. Furthermore, both rFbpA and rFbpB significantly bound to coated DPT in enzyme-linked immunosorbent assay, whereas rIII_12-14 bound to neither coated rFbpA nor rFbpB. However, rIII_12-14 marginally inhibited rFbpA and rFbpB binding to coated DPT.
In conclusion, FbpA and FbpB bound more strongly to DPT than to III_12-14, thereby inhibiting the binding of Fn and III_12-14 to DPT.