Clostridium perfringens beta-2 toxin (265 aas) forms pores in animal cells. The pore is fairly non-specific: K⁺, Ca²⁺, Na⁺ and Cl^- fluxes were measured following treatment of HL60 cells with the toxin (Nagahama et al., 2003). The toxin forms oligomeric complexes of about 191 and 228 kDa in lipid rafts.

A 120 residue region of the ε-toxin of Clostridium perfringens (TC #1.C.5.1.1) shows significant sequence similarity to the pesticidal crystal protein Cry15Aa (insecticidal δ-endotoxin CryXVA(a)), and the first 77 residues of the epsilon toxin show sequence similarity with the first 82 residues of the beta-2 toxin of C. perfringens (TC #1.C.69). Cry15Aa is not demonstrably homologous to members of the channel-forming δ-endotoxin insecticidal crystal protein (ICP) family (TC #1.C.2).

The reactions catalyzed by beta toxin are:

ions (in) ions (out)