|本期目录/Table of Contents|

[1]王佩,段明珠,黄贝,等.日本鳗鲡抗菌蛋白BPI基因的克隆、鉴定与表达[J].集美大学学报(自然科学版),2019,24(2):81-93.
 WANG Pei,DUAN Mingzhu,HUANG Bei,et al.Molecular Cloning and Expression Analysis of Two Genes Encoding Bactericidal/Permeability­Increasing Protein in Japanese Eel,Anguilla japonica[J].Journal of Jimei University,2019,24(2):81-93.
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《集美大学学报(自然科学版)》[ISSN:1007-7405/CN:35-1186/N]

卷:
第24卷
期数:
2019年第2期
页码:
81-93
栏目:
水产、食品与生物工程
出版日期:
2019-03-28

文章信息/Info

Title:
Molecular Cloning and Expression Analysis of Two Genes Encoding Bactericidal/Permeability­Increasing Protein in Japanese Eel,Anguilla japonica
作者:
王佩1段明珠1黄贝1熊静1梁英1黄文树123
(1.集美大学水产学院,福建 厦门 361021;2.鳗鲡现代产业技术教育部工程研究中心,福建 厦门 361021;3.福建省海洋生物资源开发利用协同创新中心,福建 厦门 361005)
Author(s):
WANG Pei1DUAN Mingzhu1HUANG Bei1XIONG Jing1LIANG Ying1HUANG Wenshu123
(1.Fisheries College,Jimei University,Xiamen,361021,China;2.Engineering Research Center of the Modern Technology for Eel Industry,Ministry of Education,Xiamen 361021,China;3.Fujian Collaborative Innovation Center for Development and Utilization of Marine Resources,Xiamen 361021,China)
关键词:
日本鳗鲡抗菌肽BPI基因迟缓爱德华氏菌
Keywords:
Anguilla japonicaantimicrobial peptidesbactericidal/permeability increasing protein geneEdwardsiella tarda
分类号:
-
DOI:
-
文献标志码:
A
摘要:
为探究鱼类抗菌肽—杀菌/通透性增强蛋白(bactericidal/permeability increasing protein,BPI)的功能,从日本鳗鲡(Anguilla japonica)中克隆和鉴定了两个BPI基因,命名为AJBPI-1和AJBPI-2。这两个抗菌肽均具有BPI超家族特征性的LPS结合结构域和脯氨酸富集区,其中AJBPI-1和AJBPI-2的N-端碱性氨基酸(精氨酸和赖氨酸)的数量分别为12和35,表明前者对LPS的结合力较后者弱。Real-time PCR检测结果显示,AJBPI-1在正常养殖鳗鲡的肝脏中转录表达量最高,其次是头肾,而AJBPI-2则在中肾和头肾中转录表达量最高,其次是血液。Poly I:C和E.tarda诱导后,鳗鲡脾脏中AJBPI-1和AJBPI-2的表达量均显著上调(P<0.05),AJBPI-1约为PBS对照组的4.0倍和3.3倍,AJBPI-2为PBS对照组的2.3倍和1.7倍;经LPS、Poly I:C和E.tarda刺激后,鳃中AJBPI-2表达量显著上调(P<0.05),上调幅度最高可达到PBS组的2.5倍、17.0倍和7.0倍;而中肾只在LPS和Poly I:C刺激时,AJBPI-1和AJBPI-2的表达量显著上调(P<0.05),AJBPI-1约为PBS对照组的3.0倍和2.2倍,AJBPI-2为PBS对照组的2.0倍和2.2倍。
Abstract:
In order to clarify the biological function of bactericidal/permeability-increasing protein (BPI) counterpart in teleost,two BPI genes named AJBPI-1 and AJBPI-2 have been cloned and characterized from the Japanese eel (Anguilla japonica) in this study.Both of the predicted peptides shared LPS binding domain and Pro-rich domain,and contained N-basic amino acids (arginine and lysine) which the numbers were 12 and 35,respectively,indicating the weaker binding capability of AJBPI-1 to LPS.Subsequently,their tissue specific expression was also tested by real-time PCR.Results showed that the highest expression of AJBPI-1 was liver,followed by the head kidney.However,the highest expression of AJBPI-2 was middle and head kidneys,followed by the blood.Moreover,their expressions changed in multiple tissues post different stimuli challenge were analyzed.When Poly I:C and E.tarda were used for stimulating individually,the expression levels of AJBPI-1 and AJBPI-2 in spleen were significantly up-regulated (P<0.05),which were approximately 4.0/3.3 folds and 2.3/1.7 folds than those stimulated by PBS,respectively.Only when it was stimulated by LPS,Poly I:C and E.tarda,the expression levels of AJBPI-2 in gill were significantly up-regulated (P<0.05),which were about 2.5 folds,17.0 folds and 7.0 folds,respectively.While the expression levels of AJBPI-1 and AJBPI-2 in middle kidney were significantly up-regulated after stimulation with LPS and Poly I:C (P<0.05),which were about 3.0/2.2 and 2.0/2.2 folds than those stimulated by PBS,respectively.The results will provide some data for the classification and functional analysis of BPI/LBP genes in fish.

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备注/Memo

备注/Memo:
更新日期/Last Update: 2019-05-05