Cloning of an orange-spotted grouper Epinephelus coioides heat shock protein 90AB (HSP90AB) and characterization of its expression in response to nodavirus

被引:40
作者
Chen, Young-Mao [1 ,2 ,3 ]
Kuo, Cham-En [4 ]
Wang, Ting-Yu [1 ,2 ,3 ]
Shie, Pei-Shiuan [1 ,2 ,3 ]
Wang, Wei-Chen [1 ]
Huang, Shao-Ling [1 ,2 ,3 ]
Tsai, Tieh-Jung [1 ]
Chen, Peng-Peng [1 ,2 ,3 ]
Chen, Jiann-Chu [5 ]
Chen, Tzong-Yueh [1 ,2 ,3 ]
机构
[1] Natl Cheng Kung Univ, Genet Mol Lab, Inst Biotechnol, Coll Biosci & Biotechnol, Tainan 70101, Taiwan
[2] Natl Cheng Kung Univ, Res Ctr Ocean Environm & Technol, Tainan 70101, Taiwan
[3] Natl Cheng Kung Univ, Agr Biotechnol Res Ctr, Tainan 70101, Taiwan
[4] Tzu Hui Inst Technol, Dept Nursing, Pingtung 926, Taiwan
[5] Natl Taiwan Ocean Univ, Dept Aquaculture, Chilung 202, Taiwan
关键词
HSP90AB; Nodavirus; Grouper; Geldanamycin; OXIDATIVE STRESS; GENE-EXPRESSION; RNA; CHAPERONE; CDNA; CELLS; REPLICATION; ACTIVATION; INDUCTION; INFECTION;
D O I
10.1016/j.fsi.2010.02.004
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
The heat shock proteins (HSPs) family which consists of HSP90, HSP70, and low molecular mass HSPs are involved in chaperone activity. Here, we report the cloning and characterization of HSP90AB gene from orange-spotted grouper, Epinephelus coioides. The full-length of grouper HSP90AB was 727 amino acids and possessed an ATPase domain as well as an evolutionarily conserved molecular chaperone. The HSP90AB-green fluorescent protein fusion protein was evenly distributed in the cytoplasm. Immunohistochemistry (IHC) and real-time polymerase chain reaction (PCR) analyses indicated that the expression of grouper HSP90AB was marginally increased following nodavirus infection. Grouper E. coioides that received HSP90 inhibitor geldanamycin (GA) showed an increase in HSP90AB expression and growth of nodavirus supporting nodavirus replication. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码:895 / 904
页数:10
相关论文
共 46 条
  • [1] Ackerman PA, 2001, J AQUAT ANIM HEALTH, V13, P173, DOI 10.1577/1548-8667(2001)013<0173:PACSRO>2.0.CO
  • [2] 2
  • [3] Ali A, 1996, CELL STRESS CHAPERON, V1, P62, DOI 10.1379/1466-1268(1996)001<0062:EOSIHG>2.3.CO
  • [4] 2
  • [5] [Anonymous], 2005, PHYLIP (phylogeny inference package) version 3.6
  • [6] Nodavirus RNA recombination
    Ball, LA
    [J]. SEMINARS IN VIROLOGY, 1997, 8 (02): : 95 - 100
  • [7] Heat shock protein 90 mediates macrophage activation by Taxol and bacterial lipopolysaccharide
    Byrd, CA
    Bornmann, W
    Erdjument-Bromage, H
    Tempst, P
    Pavletich, N
    Rosen, N
    Nathan, CF
    Ding, A
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (10) : 5645 - 5650
  • [8] Oxidative stress, mitochondrial dysfunction and cellular stress response in Friedreich's ataxia
    Calabrese, V
    Lodi, R
    Tonon, C
    D'Agata, V
    Sapienza, M
    Scapagnini, G
    Mangiameli, A
    Pennisi, G
    Stella, AMG
    Butterfield, DA
    [J]. JOURNAL OF THE NEUROLOGICAL SCIENCES, 2005, 233 (1-2) : 145 - 162
  • [9] Food-deprivation induces HSP70 and HSP90 protein expression in larval gilthead sea bream and rainbow trout
    Cara, JB
    Aluru, N
    Moyano, FJ
    Vijayan, MM
    [J]. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2005, 142 (04): : 426 - 431
  • [10] A functional heat shock protein 90 chaperone is essential for efficient flock house virus RNA polymerase synthesis in Drosophila cells
    Castorena, Kathryn M.
    Weeks, Spencer A.
    Stapleford, Kenneth A.
    Cadwallader, Amy M.
    Miller, David J.
    [J]. JOURNAL OF VIROLOGY, 2007, 81 (16) : 8412 - 8420