中山大学学报(自然科学版) ›› 2020, Vol. 59 ›› Issue (4): 7-18.doi: 10.13471/j.cnki.acta.snus.2019.10.18.2019E026

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澳洲宝石鲈热休克蛋白90-β基因(HSP90-β)的cDNA克隆与表达

高凇泽孙彩云吴金英叶航宇李文笙   

  1. 中山大学生命科学学院/水生经济动物研究所暨广东省水生经济动物良种繁育重点实验室/广东省重要经济鱼类健康养殖工程技术研究中心,广东 广州 510275
  • 收稿日期:2019-10-29 出版日期:2020-07-25 发布日期:2020-07-25
  • 通讯作者: 吴金英(1963年生),女;研究方向:鱼类生理和鱼类免疫学;E-mail:lsswjy@mail.sysu.edu.cn
  • 作者简介:高凇泽(1993年生),男;研究方向:鱼类生理和鱼类免疫学;E-mail:gaosz@mail2.sysu.edu.cn
  • 基金资助:


Molecular cloning and expression analysis of heat shock protein 90-β cDNA in jade perch (Scortum barcoo)

GAO Songze, SUN Caiyun, WU Jinying, YE Hangyu, LI Wensheng   

  1. Institute of Aquatic Economic Animals and Guangdong Provincial Key Laboratory for Aquatic Economic
    Animals / Guangdong Provincial Engineering Technology Research Center for Healthy Breeding of
    Important Economic Fish / School of Life Sciences, 
    Sun Yat-sen University, Guangzhou 510275, China

  • Received:2019-10-29 Online:2020-07-25 Published:2020-07-25

摘要: 热休克蛋白(heat shock proteinsHSPs)在鱼类的应激与免疫反应中起着重要的作用,HSP90-β是该家族的重要成员。为了探讨澳洲宝石鲈(Scortum barcooHSP90-β在免疫应答中的作用,本研究首次克隆得到了澳洲宝石鲈HSP90-β的全长cDNA序列。该序列长2 708 bp,其中5' UTR86 bp3' UTR444 bpORF2 178 bp,编码725个氨基酸,相对分子质量约为83 200,具有5HSP90家族的特征序列,没有信号肽序列和跨膜结构域,与其他鱼类HSP90-β氨基酸的序列一致性皆超过90%。正常情况下,澳洲宝石鲈HSP90-β mRNA主要在肝脏表达。而感染无乳链球菌(Streptococcus agalactiae)后,其在肝组织中的表达呈先降低后增加的趋势,在脾脏、头肾和脑组织则呈先上升后下降的趋势。这些结果表明澳洲宝石鲈HSP90-β可能参与了无乳链球菌感染引发的免疫反应。

关键词: 澳洲宝石鲈, HSP90-β, 分子克隆, 表达

Abstract: Heat shock proteins (HSPs) play important roles in fish stress and immune response, and HSP90-β is an important member of the HSPs family. In the present study, to investigate the possible role of HSP90-β in the immune response, the full-length cDNA sequence of HSP90-β was first cloned from jade perch (Scortum barcoo). The size of the full-length cDNA of jade perch HSP90-β is 2 708 bp, of which 5' UTR is 86 bp, 3' UTR is 444 bp, and ORF is 2 178 bp, which encodes 725 amino acids. The molecular weight of jade perch HSP90-β is predicted as 83 200. And this protein owns five characteristic sequences of the HSP90 family. Moreover, it has no signal peptide and transmembrane domain. Phylogenetic analysis showed that the amino acid sequence identity of jade perch HSP90-β is more than 90% with those of other fishes. Under normal circumstances, the HSP90-β mRNA of jade perch is mainly expressed in the liver. After infection with Streptococcus agalactiae, the HSP90-β mRNA expression decreased first and then increased in liver. Differently, it increased first and then decreased in spleen, head kidney and brain. This result suggests that the HSP90-β may be involved in the immune response elicited by S. agalactiae infection in jade perch.

Key words: Scortum barcooHSP90-β, molecular cloning, expression analysis

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