Pore-forming Pseudomonas aeruginosa cytotoxin.
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.
Xiong
G
G
Institut für Pharmakologie und Toxikologie, Justus-Liebig-Universität Giessen, Germany.
Struckmeier
M
M
Lutz
F
F
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002462:Cell Membrane / Q000187:drug effects; D002463:Cell Membrane Permeability / Q000187:drug effects; D003603:Cytotoxins / Q000737:chemistry / Q000633:toxicity*; D008969:Molecular Sequence Data; D011550:Pseudomonas aeruginosa / Q000472:pathogenicity*
D003603:Cytotoxins