Lysenin
Lysenin is a pore-forming toxin (PFT) present in the coelomic fluid of the earthworm Eisenia fetida. Pore-forming toxins are a group of proteins that act as virulence factors of several pathogenic bacteria. Lysenin proteins are chiefly involved in the defense against cellular pathogens. Following the general mechanism of action of PFTs lysenin is segregated as a soluble monomer that binds specifically to a membrane receptor, sphingomyelin in the case of lysenin. After attaching to the membrane, the oligomerization begins, resulting in a nonamer on top of membrane, known as a prepore. After a conformational change, which could be triggered by a decrease of pH, the oligomer is inserted into the membrane in the so-called pore state. Monomer Lysenin is a protein produced in the coelomocyte-leucocytes of the earthworm Eisenia fetida. This protein was first isolated from the coelomic fluid in 1996 and named lysenin (from lysis and Eisenia). Lysenin is a relatively small water-soluble molecule with a molecular weight of 33 kDa. Using X-ray crystallography, lysenin was classified as a member of the Aerolysin protein family by structure and function. Structurally, each lysenin monomer consists of a receptor binding domain (grey globular part on right of Figure 1) and a