BMB Rep. 2011; 44(6): 387-392  
Characterization of the molecular features and expression patterns of two serine proteases in Hermetia illucens (Diptera: Stratiomyidae) larvae
Wontae Kim1,2, Sungwoo Bae1, Ayoung Kim1, Kwanho Park1, Sangbeom Lee1, Youngcheol Choi1, Sangmi Han1, Younghan Park3 & Youngho Koh2,*
1National Academy of Agricultural Science, Rural Development Administration, Suwon 441-707, 2Ilsong Institute of Life Science, Hallym University, 3Department of Obstetrics and Gynecology, Hallym University Sacred Heart Hospital, Anyang 431-060, Korea
Correspondence to: Tel: 82-31-380-1857; Fax: 82-31-388-3427; E-mail: kohyh@hallym.ac.kr
Received: November 5, 2010; Accepted: April 6, 2011; Published online: June 30, 2011.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

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.
Keywords: BSF, Chymotrypsin-like protease, Hermetia illucens, Serine protease, Trypsin-like protease

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