Pore-forming Pseudomonas aeruginosa cytotoxin

Abstract

Pseudomonas aeruginosa procytotoxin protein is processed C-terminally during bacterial autolysis to generate the active 29-kDa cytotoxin molecule. Binding to target cell membranes is dependent upon Cys23 and Cys215 and a domain flanked to Cys215. On rabbit erythrocytes, cytotoxin binds to a 28-kDa peptide of a glycoprotein, its N-terminus shows high homology to channel integral membrane protein CHIP28. At concentrations of more than 3 x 10(-9) M, cytotoxin increases plasma membrane permeability 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 pseudomonal products and the resultant concept of pathogenesis is presented.