Conformation-dependent fibronectin binding to Clostridium perfringens

Nozomu Matsunaga, Riyo Aono, Kanako Okabe-Watanabe, Seiichi Katayama, Yasuo Hitsumoto.

Fibronectin (Fn), an extracellular matrix protein that is found in plasma and on the cell surface, is involved in wound healing, cell migration, and tissue reconstitution. Fn consists of 12 type I, two type II, and 15 to 17 type III modules, and has various conformations; in vitro, it has a compact or extended conformation in solutions with a low or high ionic strength, respectively. Previously, we reported that Clostridium perfringens cells bind to gelatin via Fn, and recognize Fn type III9-10 (III9-10). In the present study, we investigated the interaction between C. perfringens cells and Fn in solutions with a low (l-Fn) or high (h-Fn) ionic strength. l-Fn more bound to dry-fixed cell than h-Fn. Furthermore, Fn-prebound gelatin was prepared by reacting l-Fn or h-Fn with coated gelatin (l-Fn gelatin or h-Fn gelatin, respectively), and a substantial amount of an anti-III9-10 monoclonal antibody (HB39) and a substantial number of C. perfringens cells bound to both the l-Fn gelatin and h-Fn gelatin. However, both HB39 and C. perfringens cells showed a predilection for binding to l-Fn gelatin when compared to h-Fn gelatin. These results indicated that the Fn III9-10 modules that are recognized by C. perfringens cells are more accessible in l-Fn than in h-Fn, although C. perfringens cells can recognize both l-Fn gelatin and h-Fn gelatin. These results imply that regardless of the conformation of the reacting Fn, C. perfringens cells can efficiently adhere to collagen-binding tissues as long as Fn is bound to collagen. This may confer a major advantage for C. perfringens infection.

International Journal of Analytical Bio-Science

The Society of Analytical Bio-Science

11

1

17

24

2187-7912

https://plaza.umin.ac.jp/~e-jabs/2023-1.html