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Epsilon toxin (ETX) is produced by toxinotypes B and D of  Clostridium perfringens . It can induce lethal enterotoxemia in domestic animals, mainly in sheep, goats and cattle, causing serious economic losses to global animal husbandry. In this study, a novel and stable epsilon toxin mutant rETX Y196E -C, obtained by substituting the 196th tyrosine (Y196) with glutamic acid (E) and introducing of 23 amino acids long C-terminal peptide, was determined as a promising recombinant vaccine candidate against enterotoxemia. After the third vaccination, the antibody titers against recombinant wild type (rETX) could reach 1:10 5  in each immunized group, and the mice were completely protected from 100 × LD 50  (50% lethal dose) of rETX challenge. The mice in 15 μg subcutaneously immunized group fully survived at the dose of 500 × LD 50  of rETX challenge and 80% of mice survived at 180 μg (1000 × LD 50 ) of rETX administration.  In vitro , immune sera from 15 μg subcutaneously immunized group could completely protect MDCK cells from 16 × CT 50  (50% lethal dose of cells) of rETX challenge and protect against 10 × LD 50  dose (1.8 μg) of rETX challenge in mice. These data suggest that recombinant protein rETX Y196E -C is a potential vaccine candidate for future applied researches.

Immunization with a novel Clostridium perfringens epsilon toxin mutant rETXY196E-C confers strong protection in mice