F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.

ABSTRACT: Epsilon toxin (ETX), a potent toxin, is produced by types B and D strains of Clostridium perfringens, which could cause severe diseases in humans and domestic animals. Mutant rETX^F199E was previously demonstrated to be a good vaccine candidate. However, the mechanism concerned remains unknown. To clarify how F199E substitution reduced ETX toxicity, we performed a series of experiments. The results showed that the cell-binding and pore-forming ability of rETX^F199E was almost abolished. We speculated that F199E substitution reduced toxicity by depriving the receptor binding capability of ETX, which contributed to the hypothesis that domain I of ETX is responsible for cell binding. In addition, our data suggested that ETX could cause Ca²⁺ release from intracel

SUBMITTER: Kang J 

PROVIDER: S-EPMC5512772 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature