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Infect Immun. 1972 October; 6(4): 587-590
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Role of a Protease in Natural Activation of Clostridium botulinum Neurotoxin

Food Research Institute and Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706

ABSTRACT

All tested proteolytic Clostridium botulinum type A, B, and F strains and certain non-proteolytic B and F cultures produced a protease having trypsin-like substrate specificity; none of the tested type E (non-proteolytic) strains produced the enzyme. Progenitor toxin (toxic form whose specific toxicity is increased by treatment with trypsin) was found in culture fluid concentrates of all strains not producing the protease; it was also present in some concentrates that had the enzyme. Activation of highly purified type E progenitor toxin (molecular weight 150,000) by essentially pure protease from a proteolytic type B culture was always less than that obtained with trypsin. The product of the type E progenitor toxin-protease reaction increased in toxicity when further treated with trypsin. Results suggest that at least two bonds are cleaved by trypsin during activation of type E progenitor toxin to toxin (form manifesting maximal possible specific toxicity). Natural activation of progenitor toxin of proteolytic strains may also involve cleavage of more than one bond.

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