multiple nuclear polyhedrosis virus (AcMNPV) contains a 966 bp ORF that encodes a papain type cysteine proteinase with cathepsin L-like characteristics. Using Western blot analysis of infected cell extracts we showed that proteinase has 35.5 kDa and 32 kDa precursor forms which are processed to a 27.5 kDa mature form in a manner characteristic of papain and cathepsin L. proteinase activity was greatest under acidic conditions (pH 5.0) and was reduced in the presence of the cysteine proteinase inhibitors, leupeptin and E64. Urea, a known enhancer of cathepsin L activity, also enhanced proteinase activity. AcMNPV proteinase was detected post-mortem in tissues of insects infected with wild-type (wt) virus. Insects infected with a deletion mutant did not become flaccid after death as is normally observed with wt AcMNPV infections. These findings indicate a link between activity and degradation of host tissues during virus pathogenesis.


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