PORE-FORMING PSEUDOMONAS-AERUGINOSA CYTOTOXIN

Pseudomonas aeruginosa procytotoxin protein is processed C-terminally during bacterial autolysis to generate the active 29-kDa cytotoxin mol ecule. Binding to target cell membranes is dependent upon Cys23 and Cy s215 and a domain flanked to Cys215. On rabbit erythrocytes, cytotoxin binds to a 28-kDa peptide of a glycoprotein, its N-terminus shows hig h homology to channel integral membrane protein CHIP28. At concentrati ons of more than 3 x 10(-9) M, cytotoxin increases plasma membrane per meability of most eucaryotic cells investigated. The role of cytotoxin in the formation of pores with a diameter of 2 nm on mammalian cells is discussed. The cytotoxin effects are coordinated with other pseudom onal products and the resultant concept of pathogenesis is presented.