Heat shock 70 kDa protein cognate 5 involved in WSSV toleration of Litopenaeus vannamei

The expression levels of 97 unigenes encoding heat shock proteins of Litopenaeus vannamei was scanned, and ten of them were significantly induced by white spot syndrome virus (WSSV). Among these genes, heat shock 70 kDa protein cognate 5 (LvHSC70-5) was upregulated to the highest extent and subjecte...

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Veröffentlicht in:Developmental and comparative immunology 2017-07, Vol.72, p.9-20
Hauptverfasser: Yuan, Kai, Yuan, Feng-Hua, He, Hong-Hui, Bi, Hai-Tao, Weng, Shao-Ping, He, Jian-Guo, Chen, Yi-Hong
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container_issue
container_start_page 9
container_title Developmental and comparative immunology
container_volume 72
creator Yuan, Kai
Yuan, Feng-Hua
He, Hong-Hui
Bi, Hai-Tao
Weng, Shao-Ping
He, Jian-Guo
Chen, Yi-Hong
description The expression levels of 97 unigenes encoding heat shock proteins of Litopenaeus vannamei was scanned, and ten of them were significantly induced by white spot syndrome virus (WSSV). Among these genes, heat shock 70 kDa protein cognate 5 (LvHSC70-5) was upregulated to the highest extent and subjected to further studies. Subcellular localization assay revealed that LvHSC70-5 was located in the mitochondria. Aside from WSSV infection, unfolded protein response activation and thermal stress could also upregulate LvHSC70-5. Results of reporter gene assay demonstrated that promoter of LvHSC70-5 was activated by L. vannamei heat shock factor protein 1, activating transcription factor 4 and thermal stress. A decrease in the expression of LvHSC70-5 could reduce the aggregation of proteins in hemocytes and the cumulative mortality of WSSV-infected L. vannamei. LvHSC70-5 in L. vannamei hemocytes was upregulated by mild thermal stress. In addition, mild thermal stress, decreased the copy number of WSSV in shrimp muscle and the cumulative mortality of WSSV-infected L. vannamei. Therefore, collecting results suggested that LvHSC70-5 should be involved in WSSV toleration of shrimp L. vannamei. •LvHSC70-5 is upregulated by UPR activation and thermal stress in L. vannamei.•LvHSC70-5 is activated by L. vannamei HSF1, ATF4 and thermal stress.•LvHSC70-5 reduces the aggregation of proteins and the cumulative mortality of WSSV-infected shrimp.•Mild thermal stresses decrease the copy number of WSSV and the cumulative mortality of WSSV-infected L. vannamei.
doi_str_mv 10.1016/j.dci.2017.02.003
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Among these genes, heat shock 70 kDa protein cognate 5 (LvHSC70-5) was upregulated to the highest extent and subjected to further studies. Subcellular localization assay revealed that LvHSC70-5 was located in the mitochondria. Aside from WSSV infection, unfolded protein response activation and thermal stress could also upregulate LvHSC70-5. Results of reporter gene assay demonstrated that promoter of LvHSC70-5 was activated by L. vannamei heat shock factor protein 1, activating transcription factor 4 and thermal stress. A decrease in the expression of LvHSC70-5 could reduce the aggregation of proteins in hemocytes and the cumulative mortality of WSSV-infected L. vannamei. LvHSC70-5 in L. vannamei hemocytes was upregulated by mild thermal stress. In addition, mild thermal stress, decreased the copy number of WSSV in shrimp muscle and the cumulative mortality of WSSV-infected L. vannamei. Therefore, collecting results suggested that LvHSC70-5 should be involved in WSSV toleration of shrimp L. vannamei. •LvHSC70-5 is upregulated by UPR activation and thermal stress in L. vannamei.•LvHSC70-5 is activated by L. vannamei HSF1, ATF4 and thermal stress.•LvHSC70-5 reduces the aggregation of proteins and the cumulative mortality of WSSV-infected shrimp.•Mild thermal stresses decrease the copy number of WSSV and the cumulative mortality of WSSV-infected L. vannamei.</description><identifier>ISSN: 0145-305X</identifier><identifier>EISSN: 1879-0089</identifier><identifier>DOI: 10.1016/j.dci.2017.02.003</identifier><identifier>PMID: 28193450</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Activating transcription factor 4 ; Animals ; Arthropod Proteins - genetics ; Arthropod Proteins - metabolism ; Cloning, Molecular ; Copy number ; DNA Virus Infections - immunology ; ER-stress ; Heat shock factors ; Heat shock protein cognate 5 ; Heat shock proteins ; Heat-Shock Response ; Hemocytes ; Hemocytes - immunology ; Hot Temperature - adverse effects ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; Litopenaeus vannamei ; Localization ; Mitochondria ; Mitochondria - metabolism ; Mortality ; Muscles ; Muscles - virology ; Penaeidae - immunology ; Phylogeny ; Protein folding ; Reporter gene ; Shellfish ; Thermal stress ; Transcription Factor 4 - genetics ; Transcription Factor 4 - metabolism ; Transcriptional Activation ; Unfolded Protein Response ; Up-Regulation ; Viral Load ; Viruses ; White spot syndrome ; White spot syndrome virus ; White spot syndrome virus 1 - physiology</subject><ispartof>Developmental and comparative immunology, 2017-07, Vol.72, p.9-20</ispartof><rights>2017 Elsevier Ltd</rights><rights>Copyright © 2017 Elsevier Ltd. 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Among these genes, heat shock 70 kDa protein cognate 5 (LvHSC70-5) was upregulated to the highest extent and subjected to further studies. Subcellular localization assay revealed that LvHSC70-5 was located in the mitochondria. Aside from WSSV infection, unfolded protein response activation and thermal stress could also upregulate LvHSC70-5. Results of reporter gene assay demonstrated that promoter of LvHSC70-5 was activated by L. vannamei heat shock factor protein 1, activating transcription factor 4 and thermal stress. A decrease in the expression of LvHSC70-5 could reduce the aggregation of proteins in hemocytes and the cumulative mortality of WSSV-infected L. vannamei. LvHSC70-5 in L. vannamei hemocytes was upregulated by mild thermal stress. In addition, mild thermal stress, decreased the copy number of WSSV in shrimp muscle and the cumulative mortality of WSSV-infected L. vannamei. Therefore, collecting results suggested that LvHSC70-5 should be involved in WSSV toleration of shrimp L. vannamei. •LvHSC70-5 is upregulated by UPR activation and thermal stress in L. vannamei.•LvHSC70-5 is activated by L. vannamei HSF1, ATF4 and thermal stress.•LvHSC70-5 reduces the aggregation of proteins and the cumulative mortality of WSSV-infected shrimp.•Mild thermal stresses decrease the copy number of WSSV and the cumulative mortality of WSSV-infected L. vannamei.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>28193450</pmid><doi>10.1016/j.dci.2017.02.003</doi><tpages>12</tpages></addata></record>
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subjects Activating transcription factor 4
Animals
Arthropod Proteins - genetics
Arthropod Proteins - metabolism
Cloning, Molecular
Copy number
DNA Virus Infections - immunology
ER-stress
Heat shock factors
Heat shock protein cognate 5
Heat shock proteins
Heat-Shock Response
Hemocytes
Hemocytes - immunology
Hot Temperature - adverse effects
HSP70 Heat-Shock Proteins - genetics
HSP70 Heat-Shock Proteins - metabolism
Litopenaeus vannamei
Localization
Mitochondria
Mitochondria - metabolism
Mortality
Muscles
Muscles - virology
Penaeidae - immunology
Phylogeny
Protein folding
Reporter gene
Shellfish
Thermal stress
Transcription Factor 4 - genetics
Transcription Factor 4 - metabolism
Transcriptional Activation
Unfolded Protein Response
Up-Regulation
Viral Load
Viruses
White spot syndrome
White spot syndrome virus
White spot syndrome virus 1 - physiology
title Heat shock 70 kDa protein cognate 5 involved in WSSV toleration of Litopenaeus vannamei
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