文献类型：期刊文献

英文题名：PmPPAF is a pro-phenoloxidase activating factor involved in innate immunity response of the shrimp Penaeus monodon

作者：Ma, Tracy H. T.[1,2];Benzie, John A. H.[3,4];He, Jian-Guo[5];Sun, Cheng-Bo[1];Chan, Siuming F.[1]

机构：[1]Guangdong Ocen Univ, Coll Fisheries, Zhanjiang, Peoples R China;[2]Univ Hong Kong, Sch Biol Sci, Hong Kong, Hong Kong, Peoples R China;[3]Natl Univ Ireland Univ Coll Cork, Cork, Ireland;[4]WorldFish, Bayan Lepas 11960, Penang, Malaysia;[5]Zhongshan Univ, Sch Life Sci, Guangzhou, Guangdong, Peoples R China

年份：2014

卷号：44

期号：1

起止页码：163

外文期刊名：DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY

收录：SCI-EXPANDED(收录号：WOS:000332500900020)、、WOS

基金：The author wishes to thanks the two anonymous reviewers for their help to improve the writing of the manuscripts. This research is supported in part by the Hong Kong Research Grant Council (to SMC) and by a start up fund of the Guangdong Ocean University, PR China.

语种：英文

外文关键词：Prophenoloxidase activating system; Phenoloxidase activity; Penaeus monodon

外文摘要：One of the major steps in the innate immune response of shrimp includes the activation of serine proteinases of the pro-phenoloxidase pathway by the prophenoloxidase activation enzyme (PPAF). In this study, the cDNA encoding a serine proteinase homologue (SPH) with prophenoloxidase activating activity of Penaeus monodon (PmPPAF) was cloned and characterized. PmPPAF cDNA consists of 1444 nucleotides encoding a protein with 394 amino acid residues. The estimated molecular weight of PmPPAF is 43.5 kDa with an isoelectric point of 5.19. PmPPAF consists of a signal peptide, a CLIP domain and a carboxyl-terminal trypsin-like serine protease domain. It is highly similar to the masquerade-like protein 2A (61% similarity) of the crayfish Pacifastacus leniusculus, other serine proteases (42.9-67% identity) of P. monodon, and the PPAF of the crab (61% similarity). Unlike other SPH of P. monodon, which express mainly in the hemocytes, PmPPAF transcripts were detected in the hemocytes, eyestalk, hypodermis, gill, swimming leg and brain. Similar to the crab PPAF, PmPPAF transcript level is high in shrimp at the premolt stages and PmPPAF expression is up-regulated in shrimp infected with white spot syndrome virus (WSSV). Gene silencing of PmPPAF decreased expression of a prophenoloxidase-like gene and injection of Anti-PmPPAF antibody causes a decrease in PO activity. Taken together, these results provided evidence that PmPPAF is a serine proteinase homologue, and is involved in the pro-PO activation pathway of the shrimp innate immune system. (C) 2013 Elsevier Ltd. All rights reserved.