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Characterization of the v-cath Gene of Bombyx mori Nuclear Polyhedrosis Virus K1  

Lee, Kwang Sik (College of Natural Resources and Life Science, Dong-A University)
Li, Jianhong (College of Natural Resources and Life Science, Dong-A University)
Je, Yeon Ho (School of Agricultural Biotechnology, Seoul National University)
Woo, Soo Dong (Department of Plant Medicine, Chungbuk National University)
Sohn, Hung Dae (College of Natural Resources and Life Science, Dong-A University)
Jin, Byung Rae (College of Natural Resources and Life Science, Dong-A University)
Publication Information
International Journal of Industrial Entomology and Biomaterials / v.9, no.2, 2004 , pp. 217-223 More about this Journal
Abstract
A cathepsin L-like cysteine protease, v-cath, encoded by the baculovirus has been shown to playa role in host liquefaction. We have identified a v-cath gene in the silkworm virus, Bombyx mori nuclear polyhedrosis virus (BmNPV) K1 strain. The 969 bp v-cath has an open reading frame of 323 amino acids. A putative cleavage site and catalytic sites were conserved in BmNPV-K1 v-cath. The predicted three-dimensional structure of BmNPV-K1 v-cath revealed that the overall fold of BmNPV-K1 v-cath is similar to that of other proteases of the papain family. The deduced amino acid sequence of BmNPV-K1 v-cath showed 98% and 97% protein sequence identity to BmNPV T3 strain and to Autographa californica nuclear polyhedrosis virus, respectively. The BmNPV-K1 v-cath differed at 4 amino acid positions from BmNPV T3. The v-cath gene in BmNPV-K1 genome is located on the EcoRV 6 kb and XhoI 9 kb fragments. Northern hybridization analysis of BmNPV K1 v-cath gene revealed that it is expressed late in infection.
Keywords
Baculovirus; Bombyx mori nuclear polyhedrosis virus; Cathepsin L-like cysteine protease (v-cath); Insect cells;
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