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A galectin from shrimp Litopenaeus vannamei is involved in immune recognition and bacteria phagocytosis  ( SCI-EXPANDED收录)   被引量:51

文献类型:期刊文献

英文题名:A galectin from shrimp Litopenaeus vannamei is involved in immune recognition and bacteria phagocytosis

作者:Hou, Fujun[1];Liu, Yongjie[1];He, Shulin[1];Wang, Xianzong[1];Mao, Aitao[2];Liu, Zhigang[2];Sun, Chengbo[2];Liu, Xiaolin[1]

机构:[1]Northwest A&F Univ, Shaanxi Key Lab Mol Biol Agr, Coll Anim Sci & Technol, Yangling 712100, Peoples R China;[2]Guangdong Ocean Univ, Coll Fisheries, Guangzhou 524088, Guangdong, Peoples R China

年份:2015

卷号:44

期号:2

起止页码:584

外文期刊名:FISH & SHELLFISH IMMUNOLOGY

收录:SCI-EXPANDED(收录号:WOS:000354583800023)、、WOS

基金:This work was supported by the Agricultural Science and Technology Achievement Transformation Fund Project of Ministry of Science and Technology, China (no.2012GB2E200361), the Key Laboratory of Marine Biology, Institute of Oceanlogy, Chinese Academy of Sciences, Qianjiang distinguished experts of Hangzhou, Extension and Demonstration Program in Desalting Culture of Litopenaeus Vannamei New Breed "Ke Hai 1", Northwest A&F University, China (no. XNY2013-4) and China Scholarship Council. Comments from anonymous reviewers have greatly improved the manuscript.

语种:英文

外文关键词:Pattern recognition receptor; Galectin; Litopenaeus vannamei; Bacteria

外文摘要:Galectins are conserved family members with beta-galactosides affinity that play multiple functions in embryogenesis, development and regulation of innate and adaptive immunity. However, little functional studies were reported in crustaceans. Here, a shrimp Litopenaeus vannamei gatectin (LvGal) cDNA was identified with an open reading frame of 1017 bp, which encodes a putative protein of 338 amino acids. A carbohydrate recognition domain (CRD) and several amino acids residues involved in dimerization were found in LvGal. LvGal mRNA was mainly expressed in gills and hemocytes and upregulated post Vibrio anguillarum challenge. Recombinant LvGal (rLvGal) was expressed in Escherichia colt BL21 (DE3) and the purified rLvGal could strongly bind G(-) bacteria V. anguillarum and G(+) bacteria Micrococcus lysodeikticus. Besides, rLvGal exhibited strong activity to agglutinate V. anguillarum and weak activity to agglutinate M. lysodeikticus but no obvious antibacterial activity was found with selected bacteria. In addition, in vivo experiments showed rLvGal could promote phagocytosis of bacteria by hemocytes. Thus, through these collective data we predicted LvGal is involved in immune recognition and functions as a potential pattern recognition receptor. (c) 2015 Elsevier Ltd. All rights reserved.

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