Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila
Heat shock protein 90 (HSP90) represents a suite of highly conserved and multi-functional molecular chaperone proteins that play an important role in cellular stress responses. In order to better understand the expression of HSP90 in mollusks, a full-length complementary DNA (cDNA) of HSP90 (HcHSP90...
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doaj-0f46e9079cc846b7b2b13cbbfbe81aa92021-02-02T06:06:18ZengKeAi Communications Co., Ltd.Aquaculture and Fisheries2468-550X2017-03-0122596610.1016/j.aaf.2017.03.001Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophilaQin Wang0Junnan Wang1Guiling Wang2Congdi Wu3Jiale Li4Key Laboratory of Genetic Resources for Freshwater Aquaculture and Fisheries, Shanghai Ocean University, Shanghai 201306, ChinaKey Laboratory of Genetic Resources for Freshwater Aquaculture and Fisheries, Shanghai Ocean University, Shanghai 201306, ChinaKey Laboratory of Genetic Resources for Freshwater Aquaculture and Fisheries, Shanghai Ocean University, Shanghai 201306, ChinaKey Laboratory of Genetic Resources for Freshwater Aquaculture and Fisheries, Shanghai Ocean University, Shanghai 201306, ChinaKey Laboratory of Genetic Resources for Freshwater Aquaculture and Fisheries, Shanghai Ocean University, Shanghai 201306, ChinaHeat shock protein 90 (HSP90) represents a suite of highly conserved and multi-functional molecular chaperone proteins that play an important role in cellular stress responses. In order to better understand the expression of HSP90 in mollusks, a full-length complementary DNA (cDNA) of HSP90 (HcHSP90) was identified in Hyriopsis cumingii. HcHSP90 cDNA was 2659 bp in length, consisting of 3′ and 5′-untranslated regions and an open reading frame of 2187 bp, that encoded a 728 amino acid protein. Homology analyses showed that the HcHSP90 protein was highly conserved and had 5 well-conserved family signatures of HSP90 proteins. HcHSP90 mRNA expressed in various tissues of H. cumingii. The expression level of HcHSP90 was the highest in the digestive gland. In all tissues, with the exception of the digestive gland where it was down-regulated, HcHSP90 mRNA expression was significantly induced by temperature treatments (0, 5, 25, and 35 °C) relative to the control (15 °C). Exposure of H. cumingii to different concentrations of cadmium (50, 100, and 200 μg/L), up-regulated HcHSP90 mRNA in the haemolymph and gill but without an obvious dose-dependent response. When H. cumingii were infected with Aeromonas hydrophila, HcHSP90 mRNA expression in the haemolymph was up-regulated and peaked 36 h post-infection, while in the gills it was significantly up-regulated 3 h post-infection in the gills, then remained constant until returning to pre-challenge expression levels at 36 h post-infection. The results show that HcHSP90 expression can be significantly regulated by changes in temperature, cadmium exposure and bacterial infection. We deduced that HSP90 may play an important role in helping H. cumingii to cope with environmental stress.http://www.sciencedirect.com/science/article/pii/S2468550X17300357Hyriopsis cumingiiHSP90Sequence analysisTemperature stressCadmium exposureBacterial infection |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Qin Wang Junnan Wang Guiling Wang Congdi Wu Jiale Li |
spellingShingle |
Qin Wang Junnan Wang Guiling Wang Congdi Wu Jiale Li Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila Aquaculture and Fisheries Hyriopsis cumingii HSP90 Sequence analysis Temperature stress Cadmium exposure Bacterial infection |
author_facet |
Qin Wang Junnan Wang Guiling Wang Congdi Wu Jiale Li |
author_sort |
Qin Wang |
title |
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila |
title_short |
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila |
title_full |
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila |
title_fullStr |
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila |
title_full_unstemmed |
Molecular cloning, sequencing, and expression profiles of heat shock protein 90 (HSP90) in Hyriopsis cumingii exposed to different stressors: Temperature, cadmium and Aeromonas hydrophila |
title_sort |
molecular cloning, sequencing, and expression profiles of heat shock protein 90 (hsp90) in hyriopsis cumingii exposed to different stressors: temperature, cadmium and aeromonas hydrophila |
publisher |
KeAi Communications Co., Ltd. |
series |
Aquaculture and Fisheries |
issn |
2468-550X |
publishDate |
2017-03-01 |
description |
Heat shock protein 90 (HSP90) represents a suite of highly conserved and multi-functional molecular chaperone proteins that play an important role in cellular stress responses. In order to better understand the expression of HSP90 in mollusks, a full-length complementary DNA (cDNA) of HSP90 (HcHSP90) was identified in Hyriopsis cumingii. HcHSP90 cDNA was 2659 bp in length, consisting of 3′ and 5′-untranslated regions and an open reading frame of 2187 bp, that encoded a 728 amino acid protein. Homology analyses showed that the HcHSP90 protein was highly conserved and had 5 well-conserved family signatures of HSP90 proteins. HcHSP90 mRNA expressed in various tissues of H. cumingii. The expression level of HcHSP90 was the highest in the digestive gland. In all tissues, with the exception of the digestive gland where it was down-regulated, HcHSP90 mRNA expression was significantly induced by temperature treatments (0, 5, 25, and 35 °C) relative to the control (15 °C). Exposure of H. cumingii to different concentrations of cadmium (50, 100, and 200 μg/L), up-regulated HcHSP90 mRNA in the haemolymph and gill but without an obvious dose-dependent response. When H. cumingii were infected with Aeromonas hydrophila, HcHSP90 mRNA expression in the haemolymph was up-regulated and peaked 36 h post-infection, while in the gills it was significantly up-regulated 3 h post-infection in the gills, then remained constant until returning to pre-challenge expression levels at 36 h post-infection. The results show that HcHSP90 expression can be significantly regulated by changes in temperature, cadmium exposure and bacterial infection. We deduced that HSP90 may play an important role in helping H. cumingii to cope with environmental stress. |
topic |
Hyriopsis cumingii HSP90 Sequence analysis Temperature stress Cadmium exposure Bacterial infection |
url |
http://www.sciencedirect.com/science/article/pii/S2468550X17300357 |
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