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Molecular Cloning of a cDNA Encoding a Cathepsin B Homologue from the Mulberry Longicorn Beetle, Apriona germari  

Kim, Seong-Ryul (College of Natural Resources and Life Science, Dong-A University)
Yoon, Hyung-Joo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology)
Park, Nam-Sook (College of Natural Resources and Life Science, Dong-A University)
Lee, Sang-Mong (Department of Sericultural and Entomological Biology, Miryang National University)
Moon, Jae-Yu (College of Agriculture and Life Sciences, Seoul National University)
Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University)
Sohn, Hung-Dae (College of Natural Resources and Life Science, Dong-A University)
Publication Information
International Journal of Industrial Entomology and Biomaterials / v.4, no.1, 2002 , pp. 63-68 More about this Journal
Abstract
A cDNA encoding a putative member of cathepsin B of the thiol pretense superfamily was cloned from a cDNA library of the mulberry longicorn beetle, Apriona germari. Sequence analysis of the cDNA encoding the cathepsin B of A. germari (AgCatB) revealed that the 972 bp cDNA has an open reading frame of 324 amino acid residues. The deduced protein sequence of the AgCatB showed high homology with cathepsin B of the insects, Bombyx mori (47.3% amino acid identity), Helicoverpa armigera (46.6%) and Sarcophaga peregrina (45.6%), and the lowest homology with Aedes aegypti (33.2%). The AgCatB contains six disulfate bonds typical for cysteine pretenses. The three amino acid positions Cys-109, His-267, and Asn-287 which are conserved, active sites characteristic for cathepsin B, were also found. Phylogenetic analysis further confirmed that the AgCatB has a close relationship with that of B. mori, H. armigera and S. peregrina.
Keywords
Mulberry longicorn beetle; Apriona germari; cDNA cloning; Cathepsin B;
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