DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp
Dihydroxyacetone kinase (DAK) functions as a negative regulator of melanoma differentiation-associated gene 5 (MDA5)-mediated interferon (IFN) production in human. To explore its role in teleost fish, DAK homologue of black carp (Mylopharyngodon piceus) has been cloned and characterized in this pape...
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Veröffentlicht in: | Developmental and comparative immunology 2022-01, Vol.126, p.104255, Article 104255 |
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description | Dihydroxyacetone kinase (DAK) functions as a negative regulator of melanoma differentiation-associated gene 5 (MDA5)-mediated interferon (IFN) production in human. To explore its role in teleost fish, DAK homologue of black carp (Mylopharyngodon piceus) has been cloned and characterized in this paper. The transcription of black carp DAK (bcDAK) variated in host cells in response to LPS, poly (I:C) and virus stimulation, and bcDAK was majorly distributed in the cytoplasm. Overexpressed bcDAK in EPC cells showed little IFN promoter-inducing ability in the reporter assay and no antiviral activity in plaque assay. When co-expressed with black carp MDA5 (bcMDA5) in EPC cells, bcDAK obviously inhibited bcMDA5-mediated IFN promoter transcription in reporter assay and the antiviral activity in plaque assay. The knockdown of bcDAK enhanced the antiviral activity of the host cells. The association between bcDAK and bcMDA5 has been identified through immunofluorescent staining and co-immunoprecipitation (co-IP) assay. Thus, the data generated in this study support the conclusion that black carp DAK interacts with MDA5 and negatively regulates MDA5-mediated antiviral signaling.
1.bcDAK interacted with bcMDA5.2.Overexpressed bcDAK inhibited bcMDA5-mediated IFN signaling.3.Knocking down bcDAK enhanced host antiviral activity. |
doi_str_mv | 10.1016/j.dci.2021.104255 |
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1.bcDAK interacted with bcMDA5.2.Overexpressed bcDAK inhibited bcMDA5-mediated IFN signaling.3.Knocking down bcDAK enhanced host antiviral activity.</description><identifier>ISSN: 0145-305X</identifier><identifier>ISSN: 1879-0089</identifier><identifier>EISSN: 1879-0089</identifier><identifier>DOI: 10.1016/j.dci.2021.104255</identifier><identifier>PMID: 34487788</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Animals ; Antiviral activity ; Assaying ; Carp ; Carps ; Cytoplasm ; DAK ; Fish Diseases ; Fish Proteins - genetics ; Glycerone kinase ; Homology ; Immunity, Innate - genetics ; Immunoprecipitation ; Innate immunity ; Interferon ; Kinases ; Lipopolysaccharides ; MDA5 ; Melanoma ; Phosphotransferases (Alcohol Group Acceptor) ; Plaque assay ; Poly (I:C) ; Reoviridae - physiology ; Reoviridae Infections ; Rhabdoviridae - physiology ; Rhabdoviridae Infections ; Signaling ; SVCV ; Transcription ; Viruses</subject><ispartof>Developmental and comparative immunology, 2022-01, Vol.126, p.104255, Article 104255</ispartof><rights>2021 Elsevier Ltd</rights><rights>Copyright © 2021 Elsevier Ltd. All rights reserved.</rights><rights>Copyright Elsevier Science Ltd. Jan 2022</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-6f427c94f1268bfb8fc53d2c8584f3f3123c9488351f3517173eb901aad79d53</citedby><cites>FETCH-LOGICAL-c381t-6f427c94f1268bfb8fc53d2c8584f3f3123c9488351f3517173eb901aad79d53</cites><orcidid>0000-0002-3169-4514</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.dci.2021.104255$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34487788$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liao, Guancheng</creatorcontrib><creatorcontrib>Liu, Ji</creatorcontrib><creatorcontrib>Yin, Lijun</creatorcontrib><creatorcontrib>He, Yixuan</creatorcontrib><creatorcontrib>Qiao, Guoxia</creatorcontrib><creatorcontrib>Song, Wu</creatorcontrib><creatorcontrib>He, Yunfan</creatorcontrib><creatorcontrib>Deng, Zhuoyi</creatorcontrib><creatorcontrib>Xiao, Jun</creatorcontrib><creatorcontrib>Feng, Hao</creatorcontrib><title>DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp</title><title>Developmental and comparative immunology</title><addtitle>Dev Comp Immunol</addtitle><description>Dihydroxyacetone kinase (DAK) functions as a negative regulator of melanoma differentiation-associated gene 5 (MDA5)-mediated interferon (IFN) production in human. To explore its role in teleost fish, DAK homologue of black carp (Mylopharyngodon piceus) has been cloned and characterized in this paper. The transcription of black carp DAK (bcDAK) variated in host cells in response to LPS, poly (I:C) and virus stimulation, and bcDAK was majorly distributed in the cytoplasm. Overexpressed bcDAK in EPC cells showed little IFN promoter-inducing ability in the reporter assay and no antiviral activity in plaque assay. When co-expressed with black carp MDA5 (bcMDA5) in EPC cells, bcDAK obviously inhibited bcMDA5-mediated IFN promoter transcription in reporter assay and the antiviral activity in plaque assay. The knockdown of bcDAK enhanced the antiviral activity of the host cells. The association between bcDAK and bcMDA5 has been identified through immunofluorescent staining and co-immunoprecipitation (co-IP) assay. Thus, the data generated in this study support the conclusion that black carp DAK interacts with MDA5 and negatively regulates MDA5-mediated antiviral signaling.
1.bcDAK interacted with bcMDA5.2.Overexpressed bcDAK inhibited bcMDA5-mediated IFN signaling.3.Knocking down bcDAK enhanced host antiviral activity.</description><subject>Animals</subject><subject>Antiviral activity</subject><subject>Assaying</subject><subject>Carp</subject><subject>Carps</subject><subject>Cytoplasm</subject><subject>DAK</subject><subject>Fish Diseases</subject><subject>Fish Proteins - genetics</subject><subject>Glycerone kinase</subject><subject>Homology</subject><subject>Immunity, Innate - genetics</subject><subject>Immunoprecipitation</subject><subject>Innate immunity</subject><subject>Interferon</subject><subject>Kinases</subject><subject>Lipopolysaccharides</subject><subject>MDA5</subject><subject>Melanoma</subject><subject>Phosphotransferases (Alcohol Group Acceptor)</subject><subject>Plaque assay</subject><subject>Poly (I:C)</subject><subject>Reoviridae - physiology</subject><subject>Reoviridae Infections</subject><subject>Rhabdoviridae - physiology</subject><subject>Rhabdoviridae Infections</subject><subject>Signaling</subject><subject>SVCV</subject><subject>Transcription</subject><subject>Viruses</subject><issn>0145-305X</issn><issn>1879-0089</issn><issn>1879-0089</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1LxDAQhoMoun78AC8S8OKla6Zp2hRPi9-44kEP3kKaJpq1H2vSCv57Z1n14MHAEGbyzAt5CDkENgUG-eliWhs_TVkK2GepEBtkArIoE8ZkuUkmDDKRcCaed8hujAuGRwLbJjs8y2RRSDkhjxezO-q7V1_5IdL7i5lIWlt7PdiaRv_S6cZ3LwjQ4dVS3Q3-wwfd4KBDhPq2HTs_fNLe0arR5o0aHZb7ZMvpJtqD73uPPF1dPp3fJPOH69vz2TwxXMKQ5C5LC1NmDtJcVq6Szghep0YKmTnuOKQcX6XkAhxWAQW3VclA67ooa8H3yMk6dhn699HGQbU-Gts0urP9GFUqCgaYLQDR4z_ooh8Dfg6pnOVQljzPkII1ZUIfY7BOLYNvdfhUwNRKuFooFK5WwtVaOO4cfSePFYr73fgxjMDZGrBo4sPboKLxtjMoOVgzqLr3_8R_AVrJjgA</recordid><startdate>202201</startdate><enddate>202201</enddate><creator>Liao, Guancheng</creator><creator>Liu, Ji</creator><creator>Yin, Lijun</creator><creator>He, Yixuan</creator><creator>Qiao, Guoxia</creator><creator>Song, Wu</creator><creator>He, Yunfan</creator><creator>Deng, Zhuoyi</creator><creator>Xiao, Jun</creator><creator>Feng, Hao</creator><general>Elsevier Ltd</general><general>Elsevier Science 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>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3169-4514</orcidid></search><sort><creationdate>202201</creationdate><title>DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp</title><author>Liao, Guancheng ; Liu, Ji ; Yin, Lijun ; He, Yixuan ; Qiao, Guoxia ; Song, Wu ; He, Yunfan ; Deng, Zhuoyi ; Xiao, Jun ; Feng, Hao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-6f427c94f1268bfb8fc53d2c8584f3f3123c9488351f3517173eb901aad79d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Animals</topic><topic>Antiviral activity</topic><topic>Assaying</topic><topic>Carp</topic><topic>Carps</topic><topic>Cytoplasm</topic><topic>DAK</topic><topic>Fish Diseases</topic><topic>Fish Proteins - genetics</topic><topic>Glycerone kinase</topic><topic>Homology</topic><topic>Immunity, Innate - genetics</topic><topic>Immunoprecipitation</topic><topic>Innate immunity</topic><topic>Interferon</topic><topic>Kinases</topic><topic>Lipopolysaccharides</topic><topic>MDA5</topic><topic>Melanoma</topic><topic>Phosphotransferases (Alcohol Group Acceptor)</topic><topic>Plaque assay</topic><topic>Poly (I:C)</topic><topic>Reoviridae - physiology</topic><topic>Reoviridae Infections</topic><topic>Rhabdoviridae - physiology</topic><topic>Rhabdoviridae Infections</topic><topic>Signaling</topic><topic>SVCV</topic><topic>Transcription</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liao, Guancheng</creatorcontrib><creatorcontrib>Liu, Ji</creatorcontrib><creatorcontrib>Yin, Lijun</creatorcontrib><creatorcontrib>He, Yixuan</creatorcontrib><creatorcontrib>Qiao, Guoxia</creatorcontrib><creatorcontrib>Song, Wu</creatorcontrib><creatorcontrib>He, Yunfan</creatorcontrib><creatorcontrib>Deng, Zhuoyi</creatorcontrib><creatorcontrib>Xiao, Jun</creatorcontrib><creatorcontrib>Feng, Hao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Developmental and comparative immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liao, Guancheng</au><au>Liu, Ji</au><au>Yin, Lijun</au><au>He, Yixuan</au><au>Qiao, Guoxia</au><au>Song, Wu</au><au>He, Yunfan</au><au>Deng, Zhuoyi</au><au>Xiao, Jun</au><au>Feng, Hao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp</atitle><jtitle>Developmental and comparative immunology</jtitle><addtitle>Dev Comp Immunol</addtitle><date>2022-01</date><risdate>2022</risdate><volume>126</volume><spage>104255</spage><pages>104255-</pages><artnum>104255</artnum><issn>0145-305X</issn><issn>1879-0089</issn><eissn>1879-0089</eissn><abstract>Dihydroxyacetone kinase (DAK) functions as a negative regulator of melanoma differentiation-associated gene 5 (MDA5)-mediated interferon (IFN) production in human. To explore its role in teleost fish, DAK homologue of black carp (Mylopharyngodon piceus) has been cloned and characterized in this paper. The transcription of black carp DAK (bcDAK) variated in host cells in response to LPS, poly (I:C) and virus stimulation, and bcDAK was majorly distributed in the cytoplasm. Overexpressed bcDAK in EPC cells showed little IFN promoter-inducing ability in the reporter assay and no antiviral activity in plaque assay. When co-expressed with black carp MDA5 (bcMDA5) in EPC cells, bcDAK obviously inhibited bcMDA5-mediated IFN promoter transcription in reporter assay and the antiviral activity in plaque assay. The knockdown of bcDAK enhanced the antiviral activity of the host cells. The association between bcDAK and bcMDA5 has been identified through immunofluorescent staining and co-immunoprecipitation (co-IP) assay. Thus, the data generated in this study support the conclusion that black carp DAK interacts with MDA5 and negatively regulates MDA5-mediated antiviral signaling.
1.bcDAK interacted with bcMDA5.2.Overexpressed bcDAK inhibited bcMDA5-mediated IFN signaling.3.Knocking down bcDAK enhanced host antiviral activity.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>34487788</pmid><doi>10.1016/j.dci.2021.104255</doi><orcidid>https://orcid.org/0000-0002-3169-4514</orcidid></addata></record> |
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subjects | Animals Antiviral activity Assaying Carp Carps Cytoplasm DAK Fish Diseases Fish Proteins - genetics Glycerone kinase Homology Immunity, Innate - genetics Immunoprecipitation Innate immunity Interferon Kinases Lipopolysaccharides MDA5 Melanoma Phosphotransferases (Alcohol Group Acceptor) Plaque assay Poly (I:C) Reoviridae - physiology Reoviridae Infections Rhabdoviridae - physiology Rhabdoviridae Infections Signaling SVCV Transcription Viruses |
title | DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp |
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