Abstract：
:A cDNA encoding elastase was isolated from Steinernema carpocapsae by suppression subtractive hybridization and rapid amplification of 5' cDNA ends. The predicted protein contained a 19-aa signal peptide, a 44-aa N-terminal propeptide, and a 264-aa mature protein with a predicted molecular mass of 28,949 Da and a theoretical pI of 8.88. BLAST analysis showed 27-35% amino acid sequence identity to serine proteases from insects, mammals, fish and other organisms. The Sc-ela gene contains three exons and two introns with at least two copies in the S. carpocapsae genome. Expression analysis indicated that the Sc-ela gene was upregulated during the initial parasitic stage. Sequence comparison and evolutionary marker analysis revealed that Sc-ELA was a member of the elastase serine protease family with potential degradative, developmental and fibrinolytic activities. Homology modeling showed that Sc-ELA adopts a two beta-barrel fold typical of trypsin-like serine proteases, and phylogenetic analysis indicates that Sc-ELA branched off early during elastase evolution.
journal_name
Exp Parasitoljournal_title
Experimental parasitologyauthors
Hao YJ,Montiel R,Nascimento G,Toubarro D,Simoes Ndoi
10.1016/j.exppara.2009.01.014subject
Has Abstractpub_date
2009-05-01 00:00:00pages
51-60issue
1eissn
0014-4894issn
1090-2449pii
S0014-4894(09)00027-7journal_volume
122pub_type
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