文献类型：期刊文献

英文题名：Identification and characterization of a laccase from Litopenaeus vannamei involved in anti-bacterial host defense

作者：Shi, Lili[1];Chan, Siuming[1];Li, Chaozheng[2,3,4,5,6];Zhang, Shuang[1]

机构：[1]Guangdong Ocean Univ, Coll Fisheries, Zhanjiang 524088, Peoples R China;[2]Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, MOE Key Lab Aquat Prod Safety, Guangzhou, Guangdong, Peoples R China;[3]Sun Yat Sen Univ, Guangdong Prov Key Lab Aquat Econ Anim, Inst Aquat Econ Anim, Guangzhou, Guangdong, Peoples R China;[4]Guangdong Prov Key Lab Marine Resources & Coastal, Guangzhou, Guangdong, Peoples R China;[5]Sun Yat Sen Univ, Sch Marine Sci, Guangzhou, Guangdong, Peoples R China;[6]South China Sea Resource Exploitat & Protect Coll, Guangzhou, Guangdong, Peoples R China

年份：2017

卷号：66

起止页码：1

外文期刊名：FISH & SHELLFISH IMMUNOLOGY

收录：SCI-EXPANDED(收录号：WOS:000403986100001)、、WOS

基金：This study was supported by The PhD Start-up Fund of Natural Science Foundation of Guangdong Province, China (No. 2016A030310334 and No. 2014A030310184); Free application Fund of Natural Science Foundation of Guangdong Province, China (2016A030313757); Special support program for Outstanding Young Teachers of Guangdong Ocean University HDYQ2015004 and HDYQ2017003.

语种：英文

外文关键词：Phenoloxidase; Laccase; Litopenaeus vannamei; Immune defense

外文摘要：Phenoloxidases (POs) are a family of enzymes including tyrosinases, catecholases and laccases, which play an important role in immune defences of various invertebrates. Whether or not laccase exists in shrimp and its function is still poorly understood. In this study, a laccase (LvLac) was cloned and identified from Litopenaeus vannamei for the first time. The full length of LvLac is 3406 bp, including a 2034 bp open reading frame (ORF) coding for a putative protein of 677 amino acids with a signal peptide of 33 aa. LvLac contains three Cu-oxidase domains with copper binding centers formed by 10 histidines, one cysteine and one methionine, respectively. Phylogenetic analysis revealed that LvLac was close to insects laccase 1 family. LvLac expression was most abundant in heart and the crude LvLac protein could catalyze the oxidation of hydroquinone. Real-time PCR showed that LvLac expression was responsive to Vibrio parahaemolyticus, Micrococcus lysodeikticus and white spot syndrome virus (WSSV) infection. Knockdown of LvLac enhanced the sensitivity of shrimps to V. parahaemolyticus and M. lysodeikticus challenge, suggesting that LvLac may play a positive role against bacterial pathogens. (C) 2017 Elsevier Ltd. All rights reserved.