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Infect Immun. 1973 April; 7(4): 513-517
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Degradation of Coxsackievirus Type A9 by Proteolytic Enzymes

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

ABSTRACT

The means by which coxsackievirus type A9 (CA9) is inactivated by proteolytic enzymes was investigated. After reaction of ¹⁴C-leucine-labeled CA9 with Pronase, free leucine was liberated as measured by radiochromatography. Treatment of ¹⁴C-leucine-labeled CA9 with trypsin or proteolytic filtrates of Pseudomonas aeruginosa caused the release of a variety of labeled substances. The extent of viral ribonucleic acid (RNA) release after exposure of CA9 to Pronase was determined by RNA infectivity tests or trichloroacetic acid solubility tests. Infective viral RNA was found not to be consistently released by reaction of CA9 with Pronase, but further treatment with 1% sodium dodecyl sulfate at pH 7.0 promoted viral RNA release. Sodium dodecyl sulfate treatment of CA9 that had not been reacted with Pronase did not inactivate virus or cause viral RNA release. Reaction of Pronase with ³²P-labeled CA9 resulted in the liberation of virus components soluble in cold trichloroacetic acid, whereas untreated CA9 or CA9 reacted with ribonuclease were precipitated by cold trichloroacetic acid. These results demonstrate that the primary means by which protease-sensitive enteroviruses are inactivated is by degradation of the virus capsid, with subsequent release of viral RNA.

¹ Present address: Department of Microbiology, Harvard School of Public Health, Boston, Mass. 02115.