The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch
Heat shock protein 27 (HSP27), functioning as a stress induced protective protein, has been reported to participate in various biological processes, including apoptosis, thermal protection, and virus infection. In this study, a HSP27-like gene from the seawater fish sea perch, designated as LjHSP27,...
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description | Heat shock protein 27 (HSP27), functioning as a stress induced protective protein, has been reported to participate in various biological processes, including apoptosis, thermal protection, and virus infection. In this study, a HSP27-like gene from the seawater fish sea perch, designated as LjHSP27, was characterized. The 1361 bp full-length cDNA of LjHSP27 encoded a 221 amino acid protein containing a conserved α-crystallin domain, two variable amino- and carboxy-terminal extensions, a WD/EPF motif, two serine phosphorylation sites, and two putative actin binding regions. Phylogenetic analysis showed that LjHSP27 shared the closest genetic relationship with HSP27 of the Asian seabass Lates calcarifer. LjHSP27 mRNA was ubiquitously expressed in all tissues examined, but significantly up-regulated in spleen and kidney and down-regulated in brain post red spotted grouper nervous necrosis virus (RGNNV) infection. In vitro, LjHSP27 transcript was remarkably reduced post RGNNV infection, but rapidly increased after polyinosinic-polycytidylic acid treatment. Up-regulation and down-regulation of LjHSP27 inhibited and promoted RGNNV replication in cultured LJB cells, respectively. Luciferase assay indicated that LjHSP27 could enhance the promoter activities of zebrafish interferon (IFN)1 and IFN3, suggesting its potential role in innate immune responses. Moreover, overexpression of LjHSP27 inhibited RGNNV-induced apoptosis, as indicated by the up-regulation of anti-apoptotic genes and down-regulation of pro-apoptotic genes, while KNK437 caused down-regulation of LjHSP27 dramatically led to opposite results, suggesting that LjHSP27 might exert its anti-RGNNV activities by regulating the apoptosis signaling pathway. Our results would provide a new insight into the underlying molecular mechanism of HSP and RGNNV interaction.
•HSP27 was identified from sea perch for the first time.•LjHSP27 was involved in response to poly I:C stimulation and RGNNV infection in vitro.•LjHSP27 had an antiviral activity against RGNNV.•LjHSP27 enhanced the promoter activities of zebrafish IFN1 and IFN3.•LjHSP27 hindered the apoptosis induced by RGNNV. |
doi_str_mv | 10.1016/j.fsi.2017.08.032 |
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•HSP27 was identified from sea perch for the first time.•LjHSP27 was involved in response to poly I:C stimulation and RGNNV infection in vitro.•LjHSP27 had an antiviral activity against RGNNV.•LjHSP27 enhanced the promoter activities of zebrafish IFN1 and IFN3.•LjHSP27 hindered the apoptosis induced by RGNNV.</description><identifier>ISSN: 1050-4648</identifier><identifier>EISSN: 1095-9947</identifier><identifier>DOI: 10.1016/j.fsi.2017.08.032</identifier><identifier>PMID: 28860076</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis ; Base Sequence ; Computational Biology ; Fish Diseases - immunology ; Fish Proteins - chemistry ; Fish Proteins - genetics ; Fish Proteins - immunology ; Gene Expression Profiling - veterinary ; Gene Expression Regulation - immunology ; Heat shock protein 27 ; HSP27 Heat-Shock Proteins - chemistry ; HSP27 Heat-Shock Proteins - genetics ; HSP27 Heat-Shock Proteins - immunology ; Immunity, Innate - genetics ; Interferon ; Nervous necrosis virus ; Nodaviridae - physiology ; Perches - genetics ; Perches - immunology ; Phylogeny ; RNA Virus Infections - immunology ; Sea perch ; Sequence Alignment - veterinary</subject><ispartof>Fish & shellfish immunology, 2017-11, Vol.70, p.185-194</ispartof><rights>2017 Elsevier Ltd</rights><rights>Copyright © 2017 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-707d5ef96f69ef2dcf30efb3f6b665263d66f2967880621a02b459ca8f33328c3</citedby><cites>FETCH-LOGICAL-c353t-707d5ef96f69ef2dcf30efb3f6b665263d66f2967880621a02b459ca8f33328c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.fsi.2017.08.032$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28860076$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Le, Yao</creatorcontrib><creatorcontrib>Jia, Peng</creatorcontrib><creatorcontrib>Jin, Yilin</creatorcontrib><creatorcontrib>Liu, Wei</creatorcontrib><creatorcontrib>Jia, Kuntong</creatorcontrib><creatorcontrib>Yi, Meisheng</creatorcontrib><title>The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch</title><title>Fish & shellfish immunology</title><addtitle>Fish Shellfish Immunol</addtitle><description>Heat shock protein 27 (HSP27), functioning as a stress induced protective protein, has been reported to participate in various biological processes, including apoptosis, thermal protection, and virus infection. In this study, a HSP27-like gene from the seawater fish sea perch, designated as LjHSP27, was characterized. The 1361 bp full-length cDNA of LjHSP27 encoded a 221 amino acid protein containing a conserved α-crystallin domain, two variable amino- and carboxy-terminal extensions, a WD/EPF motif, two serine phosphorylation sites, and two putative actin binding regions. Phylogenetic analysis showed that LjHSP27 shared the closest genetic relationship with HSP27 of the Asian seabass Lates calcarifer. LjHSP27 mRNA was ubiquitously expressed in all tissues examined, but significantly up-regulated in spleen and kidney and down-regulated in brain post red spotted grouper nervous necrosis virus (RGNNV) infection. In vitro, LjHSP27 transcript was remarkably reduced post RGNNV infection, but rapidly increased after polyinosinic-polycytidylic acid treatment. Up-regulation and down-regulation of LjHSP27 inhibited and promoted RGNNV replication in cultured LJB cells, respectively. Luciferase assay indicated that LjHSP27 could enhance the promoter activities of zebrafish interferon (IFN)1 and IFN3, suggesting its potential role in innate immune responses. Moreover, overexpression of LjHSP27 inhibited RGNNV-induced apoptosis, as indicated by the up-regulation of anti-apoptotic genes and down-regulation of pro-apoptotic genes, while KNK437 caused down-regulation of LjHSP27 dramatically led to opposite results, suggesting that LjHSP27 might exert its anti-RGNNV activities by regulating the apoptosis signaling pathway. Our results would provide a new insight into the underlying molecular mechanism of HSP and RGNNV interaction.
•HSP27 was identified from sea perch for the first time.•LjHSP27 was involved in response to poly I:C stimulation and RGNNV infection in vitro.•LjHSP27 had an antiviral activity against RGNNV.•LjHSP27 enhanced the promoter activities of zebrafish IFN1 and IFN3.•LjHSP27 hindered the apoptosis induced by RGNNV.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Computational Biology</subject><subject>Fish Diseases - immunology</subject><subject>Fish Proteins - chemistry</subject><subject>Fish Proteins - genetics</subject><subject>Fish Proteins - immunology</subject><subject>Gene Expression Profiling - veterinary</subject><subject>Gene Expression Regulation - immunology</subject><subject>Heat shock protein 27</subject><subject>HSP27 Heat-Shock Proteins - chemistry</subject><subject>HSP27 Heat-Shock Proteins - genetics</subject><subject>HSP27 Heat-Shock Proteins - immunology</subject><subject>Immunity, Innate - genetics</subject><subject>Interferon</subject><subject>Nervous necrosis virus</subject><subject>Nodaviridae - physiology</subject><subject>Perches - genetics</subject><subject>Perches - immunology</subject><subject>Phylogeny</subject><subject>RNA Virus Infections - immunology</subject><subject>Sea perch</subject><subject>Sequence Alignment - veterinary</subject><issn>1050-4648</issn><issn>1095-9947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9vEzEQxS0EoqXwAbggH7nsMrazs7Y4oar8kSpxKWfL8Y4bh8062N5IfHscpXDk9GakN0_zfoy9FdALEPhh34cSewli7EH3oOQzdi3ADJ0xm_H5eR6g2-BGX7FXpewBABXCS3YltUaAEa_Z-rAj7pYaTzG7mec0E0-B78hVXnbJ_-THnCrFhcuRu0cXl1J5pomXY6q16WNO65EyXyif0lqa-pxKLLwFtjUugXyNaWkTL-R48_rda_YiuLnQmye9YT8-3z3cfu3uv3_5dvvpvvNqULUbYZwGCgYDGgpy8kEBha0KuEUcJKoJMUiDo9aAUjiQ281gvNNBKSW1Vzfs_SW3lfi1Uqn2EIuneXYLtWetMArFYCRis4qL9fx-yRTsMceDy7-tAHumbfe20bZn2ha0bbTbzbun-HV7oOnfxV-8zfDxYqBW8hQp2-IjLZ6mmBsWO6X4n_g_yDmRBw</recordid><startdate>201711</startdate><enddate>201711</enddate><creator>Le, Yao</creator><creator>Jia, Peng</creator><creator>Jin, Yilin</creator><creator>Liu, Wei</creator><creator>Jia, Kuntong</creator><creator>Yi, Meisheng</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201711</creationdate><title>The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch</title><author>Le, Yao ; Jia, Peng ; Jin, Yilin ; Liu, Wei ; Jia, Kuntong ; Yi, Meisheng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-707d5ef96f69ef2dcf30efb3f6b665263d66f2967880621a02b459ca8f33328c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Computational Biology</topic><topic>Fish Diseases - immunology</topic><topic>Fish Proteins - chemistry</topic><topic>Fish Proteins - genetics</topic><topic>Fish Proteins - immunology</topic><topic>Gene Expression Profiling - veterinary</topic><topic>Gene Expression Regulation - immunology</topic><topic>Heat shock protein 27</topic><topic>HSP27 Heat-Shock Proteins - chemistry</topic><topic>HSP27 Heat-Shock Proteins - genetics</topic><topic>HSP27 Heat-Shock Proteins - immunology</topic><topic>Immunity, Innate - genetics</topic><topic>Interferon</topic><topic>Nervous necrosis virus</topic><topic>Nodaviridae - physiology</topic><topic>Perches - genetics</topic><topic>Perches - immunology</topic><topic>Phylogeny</topic><topic>RNA Virus Infections - immunology</topic><topic>Sea perch</topic><topic>Sequence Alignment - veterinary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Le, Yao</creatorcontrib><creatorcontrib>Jia, Peng</creatorcontrib><creatorcontrib>Jin, Yilin</creatorcontrib><creatorcontrib>Liu, Wei</creatorcontrib><creatorcontrib>Jia, Kuntong</creatorcontrib><creatorcontrib>Yi, Meisheng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Fish & shellfish immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Le, Yao</au><au>Jia, Peng</au><au>Jin, Yilin</au><au>Liu, Wei</au><au>Jia, Kuntong</au><au>Yi, Meisheng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch</atitle><jtitle>Fish & shellfish immunology</jtitle><addtitle>Fish Shellfish Immunol</addtitle><date>2017-11</date><risdate>2017</risdate><volume>70</volume><spage>185</spage><epage>194</epage><pages>185-194</pages><issn>1050-4648</issn><eissn>1095-9947</eissn><abstract>Heat shock protein 27 (HSP27), functioning as a stress induced protective protein, has been reported to participate in various biological processes, including apoptosis, thermal protection, and virus infection. In this study, a HSP27-like gene from the seawater fish sea perch, designated as LjHSP27, was characterized. The 1361 bp full-length cDNA of LjHSP27 encoded a 221 amino acid protein containing a conserved α-crystallin domain, two variable amino- and carboxy-terminal extensions, a WD/EPF motif, two serine phosphorylation sites, and two putative actin binding regions. Phylogenetic analysis showed that LjHSP27 shared the closest genetic relationship with HSP27 of the Asian seabass Lates calcarifer. LjHSP27 mRNA was ubiquitously expressed in all tissues examined, but significantly up-regulated in spleen and kidney and down-regulated in brain post red spotted grouper nervous necrosis virus (RGNNV) infection. In vitro, LjHSP27 transcript was remarkably reduced post RGNNV infection, but rapidly increased after polyinosinic-polycytidylic acid treatment. Up-regulation and down-regulation of LjHSP27 inhibited and promoted RGNNV replication in cultured LJB cells, respectively. Luciferase assay indicated that LjHSP27 could enhance the promoter activities of zebrafish interferon (IFN)1 and IFN3, suggesting its potential role in innate immune responses. Moreover, overexpression of LjHSP27 inhibited RGNNV-induced apoptosis, as indicated by the up-regulation of anti-apoptotic genes and down-regulation of pro-apoptotic genes, while KNK437 caused down-regulation of LjHSP27 dramatically led to opposite results, suggesting that LjHSP27 might exert its anti-RGNNV activities by regulating the apoptosis signaling pathway. Our results would provide a new insight into the underlying molecular mechanism of HSP and RGNNV interaction.
•HSP27 was identified from sea perch for the first time.•LjHSP27 was involved in response to poly I:C stimulation and RGNNV infection in vitro.•LjHSP27 had an antiviral activity against RGNNV.•LjHSP27 enhanced the promoter activities of zebrafish IFN1 and IFN3.•LjHSP27 hindered the apoptosis induced by RGNNV.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>28860076</pmid><doi>10.1016/j.fsi.2017.08.032</doi><tpages>10</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Apoptosis Base Sequence Computational Biology Fish Diseases - immunology Fish Proteins - chemistry Fish Proteins - genetics Fish Proteins - immunology Gene Expression Profiling - veterinary Gene Expression Regulation - immunology Heat shock protein 27 HSP27 Heat-Shock Proteins - chemistry HSP27 Heat-Shock Proteins - genetics HSP27 Heat-Shock Proteins - immunology Immunity, Innate - genetics Interferon Nervous necrosis virus Nodaviridae - physiology Perches - genetics Perches - immunology Phylogeny RNA Virus Infections - immunology Sea perch Sequence Alignment - veterinary |
title | The antiviral role of heat shock protein 27 against red spotted grouper nervous necrosis virus infection in sea perch |
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