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Molecular cloning and characterization of a novel pathogen‐induced trypsin‐like protease in S cylla paramamosain (Estampador 1949)
Author(s) -
Ding Jian,
Peng Hui,
Cui Qian,
Wang KeJian
Publication year - 2015
Publication title -
aquaculture research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.646
H-Index - 89
eISSN - 1365-2109
pISSN - 1355-557X
DOI - 10.1111/are.12225
Subject(s) - scylla paramamosain , key (lock) , china , chinese academy of sciences , cloning (programming) , biology , ecology , geography , archaeology , genetics , computer science , gene , programming language
Serine protease (SP) is one of the oldest characterized and largest multigene proteolytic families, in which serine serves as the nucleophilic amino acid at the catalytic site. The active serine and two other residues (a histidine and an aspartate) are referred to as the ‘catalytic triad’ in the catalytic sites of many families of SP including trypsin (S1), alpha-lytic endopeptidases (S2), togavirus endopeptidase (S3), subtilisn (S8), prolyl oligopeptidase (S9) and serine carboxypeptidase (S10) families (Rawlings & Barrett 1993). In the trypsin subfamily, the three residues, serine, histidine and aspartate are, respectively, surrounded by ‘GDSGGP’, ‘TAAHC’ and ‘DIMLL’, which are all highly conserved motifs (Yousef, Elliott, Kopolovic, Serry & Diamandis 2004). Serine protease homologs (SPHs) are similar in amino acid sequence to S1 family SPs, but apparently lack amidase activity because the mutation of one or more of the catalytic residues (Ross, Jiang, Kanost & Wang 2003). In invertebrates, arthropod SPs and SPHs are probably involved in various immune responses including haemolymph coagulation, melanotic encapsulation, induction of antimicrobial peptide synthesis and activation of cytokines by constituting a complex enzyme system in haemolymph (Ross et al. 2003; Piao, Kim, Kim, Park, Lee & Ha 2007). Melanization is an important immune response in many invertebrates and its (prephenoloxidase activating) cascade is regulated by SPs including the proPO-activating enzyme (PPAE), and SPHs (Cerenius, Lee & S€ oderh€ all 2008). PPAE is the final link in the cascade leading to PO activation and keep it under tight control by another proteinase, their cofactors (non-catalytic serine proteinase homologues) and serine proteinase inhibitors. All those proteinases can properly be referred to as prophenoloxidase-activating factors (PPAF) (Buda & Shafer 2005). Many PPAE genes encoding either serine proteases (SPs) or serine protease homologs (SPHs) have been cloned and identified from a variety of arthropod species such as Holotrichia diomphalia (Kwon, Kim, Choi, Joo, Cho & Lee 2000; Kim, Baek, Lee, Park, Lee, S€ oderh€ all & Lee 2002), Manduca sexta (Jiang, Wang & Kanost 1998; Yu, Jiang, Wang & Kanost 2003; Gupta, Wang & Jiang 2005), the crayfish Pacifastacus leniusculus (Wang, Jiang & Kanost 2001), the black tiger shrimp Penaeus monodon (Amparyup, Jitvaropas, Pulsook & Tassanakajon 2007; Charoensapsri, Amparyup, Hirono, Aoki & Tassanakajon 2011), Chinese mitten crab Eriocheir sinensis (Gai, Qiu, Wang, Song, Mu, Zhao, Zhang & Li 2009), the swimming crab Portunus trituberculatus (Cui, Liu, Wu, Luan, Wang, Li & Song 2010) and Fenneropenaeus indicus (Vaseeharan, Shanthi & Prabhu 2011). Most of the reported SPs have multi-domains such as H.diomphalia PPAF-1 and HP-14. The H.diomphalia PPAF-1 consists of clip and chymotrypsin-like domains (Lee, Kwon, Hyun, Choi, Kawabata, Iwanaga & Lee 1998; Piao et al. 2007), while HP-14 is an upstream proteinase from the moth Manduca sexta containing five low density lipoprotein receptor class A repeats, a Sushi domain, a unique Cys-rich region and a proteinase-catalytic domain (Ji, Wang, Guo, Hartson & Jiang 2004).