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)
  • Published : 2002.03.01

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

References

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