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

Young Mao Chen; Cham En Kuo; Ting Yu Wang; Pei Shiuan Shie; Wei Chen Wang; Shao Ling Huang; Tieh Jung Tsai; Peng Peng Chen; Jiann Chu Chen; Tzong Yueh Chen

doi:10.1016/j.fsi.2010.02.004

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

Young Mao Chen, Cham En Kuo, Ting Yu Wang, Pei Shiuan Shie, Wei Chen Wang, Shao Ling Huang, Tieh Jung Tsai, Peng Peng Chen, Jiann Chu Chen, Tzong Yueh Chen

Department of Biotechnology and Bioindustry Sciences

Research output: Contribution to journal › Article › peer-review

44 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	895-904
Number of pages	10
Journal	Fish and Shellfish Immunology
Volume	28
Issue number	5-6
DOIs	https://doi.org/10.1016/j.fsi.2010.02.004
Publication status	Published - 2010

All Science Journal Classification (ASJC) codes

Environmental Chemistry
Immunology
Aquatic Science
Immunology and Microbiology (miscellaneous)

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10.1016/j.fsi.2010.02.004

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Chen, Y. M., Kuo, C. E., Wang, T. Y., Shie, P. S., Wang, W. C., Huang, S. L., Tsai, T. J., Chen, P. P., Chen, J. C., & Chen, T. Y. (2010). Cloning of an orange-spotted grouper Epinephelus coioides heat shock protein 90AB (HSP90AB) and characterization of its expression in response to nodavirus. Fish and Shellfish Immunology, 28(5-6), 895-904. https://doi.org/10.1016/j.fsi.2010.02.004

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

abstract = "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.",

author = "Chen, {Young Mao} and Kuo, {Cham En} and Wang, {Ting Yu} and Shie, {Pei Shiuan} and Wang, {Wei Chen} and Huang, {Shao Ling} and Tsai, {Tieh Jung} and Chen, {Peng Peng} and Chen, {Jiann Chu} and Chen, {Tzong Yueh}",

note = "Funding Information: We thank Dr. Brian D Hoyle for reading the manuscript. This research was supported by the National Science and Technology Program for Agricultural Biotechnology, Council of Agriculture (97AS-1.2.1-ST-a3(23)), and National Science Council ( NSC96-2317-B-006-002 ), and the Landmark Project ( B0127 ) of National Cheng Kung University, the plan of University Advancement, Ministry of Education.",

year = "2010",

doi = "10.1016/j.fsi.2010.02.004",

language = "English",

volume = "28",

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AU - Chen, Young Mao

AU - Kuo, Cham En

AU - Wang, Ting Yu

AU - Shie, Pei Shiuan

AU - Wang, Wei Chen

AU - Huang, Shao Ling

AU - Tsai, Tieh Jung

AU - Chen, Peng Peng

AU - Chen, Jiann Chu

AU - Chen, Tzong Yueh

N1 - Funding Information: We thank Dr. Brian D Hoyle for reading the manuscript. This research was supported by the National Science and Technology Program for Agricultural Biotechnology, Council of Agriculture (97AS-1.2.1-ST-a3(23)), and National Science Council ( NSC96-2317-B-006-002 ), and the Landmark Project ( B0127 ) of National Cheng Kung University, the plan of University Advancement, Ministry of Education.

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

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

Abstract

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