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Infection and Immunity logoLink to Infection and Immunity
. 1977 Apr;16(1):353–361. doi: 10.1128/iai.16.1.353-361.1977

Structure-activity relationships of an exotoxin of Pseudomonas aeruginosa.

M L Vasil, D Kabat, B H Iglewski
PMCID: PMC421528  PMID: 406204

Abstract

The relation of the structure of Pseudomonas 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 its 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.

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Selected References

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