作者: Yunchao Gai , Limei Qiu , Lingling Wang , Linsheng Song , Changkao Mu
DOI: 10.1016/J.FSI.2009.08.005
关键词: Biology 、 Serine protease 、 Expressed sequence tag 、 Serine 、 Complementary DNA 、 Eriocheir 、 Molecular biology 、 Listonella anguillarum 、 Open reading frame 、 Untranslated region
摘要: Clip domain serine protease (cSP), characterized by conserved clip domains, is a new family identified mainly in arthropod, and plays important roles development immunity. In the present study, full-length cDNA of cSP (designated EscSP) was cloned from Chinese mitten crab Eriocheir sinensis expressed sequence tags (ESTs) PCR techniques. The 1380 bp EscSP contained 1152 open reading frame (ORF) encoding putative 383 amino acids, 5'-untranslated region (UTR) 54 bp, 3'-UTR 174 bp. Multiple alignment presented twelve cysteine residues canonical catalytic triad (His(185), Asp(235) Ser(332)) critical for fundamental structure function EscSP. Two types tryp_spc domain, were deduced acids conservation characteristics similarities with previously known cSPs indicated that member large family. mRNA expression different tissues temporal haemocytes challenged Listonella anguillarum measured real-time RT-PCR. transcripts could be detected all examined tissues, higher muscle than hepatopancreas. gill, gonad, heart. up-regulated after L challenge peaked at 2 h (4.96 fold, P < 0.05) 12 (9.90 0.05). Its pattern similar to prophenoloxidase (EsproPO), one components proPO system found our previous report. These results implied involved processes host-pathogen interaction probably as members. (C) 2009 Elsevier Ltd. All rights reserved.