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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae

  • Kim, Won-Tae (National Academy of Agricultural Science, Rural Development Administration) ;
  • Bae, Sung-Woo (National Academy of Agricultural Science, Rural Development Administration) ;
  • Kim, A-Young (National Academy of Agricultural Science, Rural Development Administration) ;
  • Park, Kwan-Ho (National Academy of Agricultural Science, Rural Development Administration) ;
  • Lee, Sang-Beom (National Academy of Agricultural Science, Rural Development Administration) ;
  • Choi, Young-Cheol (National Academy of Agricultural Science, Rural Development Administration) ;
  • Han, Sang-Mi (National Academy of Agricultural Science, Rural Development Administration) ;
  • Park, Young-Han (Department of Obstetrics and Gynecology, Hallym University Sacred Heart Hospital) ;
  • Koh, Young-Ho (Ilsong Institute of Life Science, Hallym University)
  • Received : 2010.11.05
  • Accepted : 2011.04.06
  • Published : 2011.06.30
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Abstract

To investigate the molecular scavenging capabilities of the larvae of Hermetia illucens, two serine proteases (SPs) were cloned and characterized. Multiple sequence alignments and phylogenetic tree analysis of the deduced amino acid sequences of Hi-SP1 and Hi-SP2 were suggested that Hi-SP1 may be a chymotrypsin- and Hi-SP2 may be a trypsin-like protease. Hi-SP1 and Hi-SP2 3-D homology models revealed that a catalytic triad, three disulfide bonds, and a substrate-binding pocket were highly conserved, as would be expected of a SP. E. coli expressed Hi-SP1 and Hi-SP2 showed chymotrypsin or trypsin activities, respectively. Hi-SP2 mRNAs were consistently expressed during larval development. In contrast, the expression of Hi-SP1 mRNA fluctuated between feeding and molting stages and disappeared at the pupal stages. These expression pattern differences suggest that Hi-SP1 may be a larval specific chymotrypsin-like protease involved with food digestion, while Hi-SP2 may be a trypsin-like protease with diverse functions at different stages.

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References

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