@article{mbs:/content/journal/jgv/10.1099/0022-1317-76-5-1091, author = "Slack, Jeffrey M. and Kuzio, John and Faulkner, Peter", title = "Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus Autographa californica multiple nuclear polyhedrosis virus", journal= "Journal of General Virology", year = "1995", volume = "76", number = "5", pages = "1091-1098", doi = "https://doi.org/10.1099/0022-1317-76-5-1091", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-76-5-1091", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = " Autographa californica 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 v-cath 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. V-cath 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 v-cath proteinase activity. AcMNPV v-cath proteinase was detected post-mortem in tissues of insects infected with wild-type (wt) virus. Insects infected with a v-cath deletion mutant did not become flaccid after death as is normally observed with wt AcMNPV infections. These findings indicate a link between v-cath activity and degradation of host tissues during virus pathogenesis.", }