TSO LING CHEN¹, LEE CHUNG LIN², JAULANG HWANG³ and CHIA PO LIN^1,2

ABSTRACT

   It is well known that a number of toxins produced by bacteria exert their action by ADP-ribosylating reaction to certain proteins which are essential for normal eukaryotic cellular functions. Most of these toxins are composed of two moieties, A and B. The B moiety mediates the binding to the specific receptor on the surface of toxin-sensitive cells, while the A moiety is responsible for the enzymatic ADP-ribosylating activity. Pseudomonas exotoxin A (PEA) is the most toxic component of the extracellular products produced by Pseudomonas aeruginosa. The three domain model of PEA has been well established : domain I, domain II, and domain III exerting binding, translocation, and ADP-ribosylating activities, respectively. Because of the cytotoxic ADP-ribosylating nature of PEA, it has been suggested as a good candidate in the preparation of immunotoxins. In this minireview article, we discuss the structure and function of the bacterial ADP-ribosylating toxins including PEA and compare the differences particularly between PEA and other valevant toxins.