The relation of the structure of P. aeruginosa exotoxin A (PA toxin) to its enzymatic activity (adenosine 5'-diphosphate-ribosyl transferase) in vitro and to its toxicity in vivo was examined. PA toxin is produced as a single polypeptide chain with a molecular weight of about 71,500. PA toxin is produced by Pseudomonas as a toxic proenzyme that lacks enzymatic activity. Adenosine 5'-diphosphate- ribosyl transferase activity is expressed when the molecule is denatured and reduced or when it is cleaved by Pseudomonas proteases to yield an enzymatically active 27,000-dalton fragment (fragment a). A 45,000-dalton protein is tentatively identified as the enzymatically inactive fragment b of PA toxin. Enzymatically active forms of the toxin lack toxicity for mouse L-cells or mouse lethality. Thus, it is concluded that the native toxin proenzyme is required for toxicity and that a structural rearrangement must precede its intracellular activity.
|Original language||English (US)|
|Number of pages||9|
|Journal||Infection and Immunity|
|State||Published - Dec 1 1977|
ASJC Scopus subject areas
- Infectious Diseases