Functional and pathogenic analysis of carbohydrate-active enzymes from Clostridium perfirngens
Japan Society for the Promotion of Science:Grants-in-Aid for Scientific Research
Date (from‐to) : 2012/04 -2015/03
Author : MIYATA Shigeru; MORIYAMA Ryuichi; OKABE Akinobu; NARIYA Hirofumi; YOSHIDA Hiromi; NAKAKITA Shinichi
Clostridium perfringens is notable for their genomic content of numerous open-reading frames that encode carbohydrate-active enzymes. Among them, hyaluronidase is thought to function as virulence factors. This enzyme is believed to spread the organism in infected tissues or potentiate other toxins through facilitation of their diffusion via the degradation of hyaluronan, NagH has been partially purified as hyaluronidase from the organism (Canard, et al., 1994).
In this study, we successfully purified NagH and the products of nagH paralogs, NagI, NagJ, NagK and NagL with high quality from recombinant C. perfringens cultures. These recombinant enzymes exhibit exo-N-acetyl-β-glucosaminidase activity but not hyaluronan degrading activity. These results led us question whether C. perfringens Nag(s) could genuinely hydrolyze hyaluronan. Thus, we searched and found a genuine gene of hyaluronidase in the organism, and indicated that the product exhibits hyaluronan degrading activity.