TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation
Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3–6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation o...
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| creator | Wang, Suyan Yu, Mengmeng Liu, Aijing Bao, Yuanling Qi, Xiaole Gao, Li Chen, Yuntong Liu, Peng Wang, Yulong Xing, Lixiao Meng, Lingzhai Zhang, Yu Fan, Linjin Li, Xinyi Pan, Qing Zhang, Yanping Cui, Hongyu Li, Kai Liu, Changjun He, Xijun Gao, Yulong Wang, Xiaomei |
| description | Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3–6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV
in vitro
and
in vivo
. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3. |
| doi_str_mv | 10.1371/journal.ppat.1009900 |
| format | Article |
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in vitro
and
in vivo
. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1009900</identifier><identifier>PMID: 34516573</identifier><language>eng</language><publisher>San Francisco: Public Library of Science</publisher><subject>Avian cells ; Barriers ; Binding proteins ; Biology and Life Sciences ; Care and treatment ; Degradation ; Dengue fever ; Development and progression ; Diseases ; Double-stranded RNA ; Experiments ; Genetic aspects ; Genomes ; Health aspects ; Host-virus relationships ; Immune system ; Immunoprecipitation ; Immunosuppression ; Infections ; Infectious bursal disease ; Medicine and Health Sciences ; Physiological aspects ; Poultry ; Proteasomes ; Proteins ; Replication ; Research and analysis methods ; RNA polymerase ; RNA virus infections ; RNA viruses ; Standard deviation ; Ubiquitin-proteasome system ; Ubiquitination ; Viral infections ; Viral proteins ; Viruses ; VP3 protein</subject><ispartof>PLoS pathogens, 2021-09, Vol.17 (9), p.e1009900-e1009900</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>2021 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 Wang et al 2021 Wang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c638t-35a0ae944463dab734aa37b3236474e3181d26512adbc3ceaa69a9cd4f5588163</citedby><cites>FETCH-LOGICAL-c638t-35a0ae944463dab734aa37b3236474e3181d26512adbc3ceaa69a9cd4f5588163</cites><orcidid>0000-0001-5887-9239 ; 0000-0003-4751-8053 ; 0000-0001-7411-9184</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8459960/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8459960/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids></links><search><contributor>Mounce, Bryan</contributor><creatorcontrib>Wang, Suyan</creatorcontrib><creatorcontrib>Yu, Mengmeng</creatorcontrib><creatorcontrib>Liu, Aijing</creatorcontrib><creatorcontrib>Bao, Yuanling</creatorcontrib><creatorcontrib>Qi, Xiaole</creatorcontrib><creatorcontrib>Gao, Li</creatorcontrib><creatorcontrib>Chen, Yuntong</creatorcontrib><creatorcontrib>Liu, Peng</creatorcontrib><creatorcontrib>Wang, Yulong</creatorcontrib><creatorcontrib>Xing, Lixiao</creatorcontrib><creatorcontrib>Meng, Lingzhai</creatorcontrib><creatorcontrib>Zhang, Yu</creatorcontrib><creatorcontrib>Fan, Linjin</creatorcontrib><creatorcontrib>Li, Xinyi</creatorcontrib><creatorcontrib>Pan, Qing</creatorcontrib><creatorcontrib>Zhang, Yanping</creatorcontrib><creatorcontrib>Cui, Hongyu</creatorcontrib><creatorcontrib>Li, Kai</creatorcontrib><creatorcontrib>Liu, Changjun</creatorcontrib><creatorcontrib>He, Xijun</creatorcontrib><creatorcontrib>Gao, Yulong</creatorcontrib><creatorcontrib>Wang, Xiaomei</creatorcontrib><title>TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation</title><title>PLoS pathogens</title><description>Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3–6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV
in vitro
and
in vivo
. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.</description><subject>Avian cells</subject><subject>Barriers</subject><subject>Binding proteins</subject><subject>Biology and Life Sciences</subject><subject>Care and treatment</subject><subject>Degradation</subject><subject>Dengue fever</subject><subject>Development and progression</subject><subject>Diseases</subject><subject>Double-stranded RNA</subject><subject>Experiments</subject><subject>Genetic aspects</subject><subject>Genomes</subject><subject>Health aspects</subject><subject>Host-virus relationships</subject><subject>Immune system</subject><subject>Immunoprecipitation</subject><subject>Immunosuppression</subject><subject>Infections</subject><subject>Infectious bursal disease</subject><subject>Medicine and Health Sciences</subject><subject>Physiological aspects</subject><subject>Poultry</subject><subject>Proteasomes</subject><subject>Proteins</subject><subject>Replication</subject><subject>Research and analysis methods</subject><subject>RNA polymerase</subject><subject>RNA virus infections</subject><subject>RNA viruses</subject><subject>Standard deviation</subject><subject>Ubiquitin-proteasome system</subject><subject>Ubiquitination</subject><subject>Viral infections</subject><subject>Viral proteins</subject><subject>Viruses</subject><subject>VP3 protein</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqVkllv1DAQxyMEoqXwDZCIxAs87GJnfCQvSFXFsVI5VAqv1vhI6lU23tpJRb893m5ALOoLsiXb49_87TmK4jklSwqSvlmHKQ7YL7dbHJeUkKYh5EFxTDmHhQTJHv61PyqepLQmhFGg4nFxBIxTwSUcF-HyYvWp4qUfrrz2Y8qb1pnRhymVeooJ-9L65DC58sbHbIxu23uDmRhKfVuOGDs3-qErf3yFsg2xnLS_nnw27RkcbGldF9HenZ8Wj1rsk3s2ryfF9_fvLs8-Ls6_fFidnZ4vjIB6XABHgq5hjAmwqCUwRJAaKhBMMge0prYSnFZotQHjEEWDjbGs5byuqYCT4sVed9uHpOZcJVXxOk_ByI5Y7QkbcK220W8w3qqAXt0ZQuwUxtGb3inbSlPXujam1sxJqyuJBiTYVhiNeqf1dn5t0htnjRvGiP2B6OHN4K9UF25UzXjTCJIFXs0CMVxPLo1q45NxfY-Dy6XI_5YVB5C8yujLf9D7o5upDnMAuaghv2t2oupUSMlJ1dSQqeU9VB7WbbwJg2t9th84vD5wyMzofo4dTimp1beL_2A_H7Jsz5oYUoqu_ZM7StSu3X8HqXbtruZ2h18JovL8</recordid><startdate>20210913</startdate><enddate>20210913</enddate><creator>Wang, 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inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation</title><author>Wang, Suyan ; Yu, Mengmeng ; Liu, Aijing ; Bao, Yuanling ; Qi, Xiaole ; Gao, Li ; Chen, Yuntong ; Liu, Peng ; Wang, Yulong ; Xing, Lixiao ; Meng, Lingzhai ; Zhang, Yu ; Fan, Linjin ; Li, Xinyi ; Pan, Qing ; Zhang, Yanping ; Cui, Hongyu ; Li, Kai ; Liu, Changjun ; He, Xijun ; Gao, Yulong ; Wang, Xiaomei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c638t-35a0ae944463dab734aa37b3236474e3181d26512adbc3ceaa69a9cd4f5588163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Avian cells</topic><topic>Barriers</topic><topic>Binding proteins</topic><topic>Biology and Life Sciences</topic><topic>Care and treatment</topic><topic>Degradation</topic><topic>Dengue fever</topic><topic>Development and progression</topic><topic>Diseases</topic><topic>Double-stranded RNA</topic><topic>Experiments</topic><topic>Genetic aspects</topic><topic>Genomes</topic><topic>Health aspects</topic><topic>Host-virus relationships</topic><topic>Immune system</topic><topic>Immunoprecipitation</topic><topic>Immunosuppression</topic><topic>Infections</topic><topic>Infectious bursal disease</topic><topic>Medicine and Health Sciences</topic><topic>Physiological aspects</topic><topic>Poultry</topic><topic>Proteasomes</topic><topic>Proteins</topic><topic>Replication</topic><topic>Research and analysis methods</topic><topic>RNA polymerase</topic><topic>RNA virus infections</topic><topic>RNA viruses</topic><topic>Standard deviation</topic><topic>Ubiquitin-proteasome system</topic><topic>Ubiquitination</topic><topic>Viral infections</topic><topic>Viral proteins</topic><topic>Viruses</topic><topic>VP3 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Suyan</creatorcontrib><creatorcontrib>Yu, 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for ubiquitination and degradation</atitle><jtitle>PLoS pathogens</jtitle><date>2021-09-13</date><risdate>2021</risdate><volume>17</volume><issue>9</issue><spage>e1009900</spage><epage>e1009900</epage><pages>e1009900-e1009900</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Infectious bursal disease virus (IBDV), a double-stranded RNA virus, causes immunosuppression and high mortality in 3–6-week-old chickens. Innate immune defense is a physical barrier to restrict viral replication. After viral infection, the host shows crucial defense responses, such as stimulation of antiviral effectors to restrict viral replication. Here, we conducted RNA-seq in avian cells infected by IBDV and identified TRIM25 as a host restriction factor. Specifically, TRIM25 deficiency dramatically increased viral yields, whereas overexpression of TRIM25 significantly inhibited IBDV replication. Immunoprecipitation assays indicated that TRIM25 only interacted with VP3 among all viral proteins, mediating its K27-linked polyubiquitination and subsequent proteasomal degradation. Moreover, the Lys854 residue of VP3 was identified as the key target site for the ubiquitination catalyzed by TRIM25. The ubiquitination site destroyed enhanced the replication ability of IBDV
in vitro
and
in vivo
. These findings demonstrated that TRIM25 inhibited IBDV replication by specifically ubiquitinating and degrading the structural protein VP3.</abstract><cop>San Francisco</cop><pub>Public Library of Science</pub><pmid>34516573</pmid><doi>10.1371/journal.ppat.1009900</doi><orcidid>https://orcid.org/0000-0001-5887-9239</orcidid><orcidid>https://orcid.org/0000-0003-4751-8053</orcidid><orcidid>https://orcid.org/0000-0001-7411-9184</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | PLoS pathogens, 2021-09, Vol.17 (9), p.e1009900-e1009900 |
| issn | 1553-7374 1553-7366 1553-7374 |
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| source | DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central Open Access; Public Library of Science (PLoS) Journals Open Access; PubMed Central |
| subjects | Avian cells Barriers Binding proteins Biology and Life Sciences Care and treatment Degradation Dengue fever Development and progression Diseases Double-stranded RNA Experiments Genetic aspects Genomes Health aspects Host-virus relationships Immune system Immunoprecipitation Immunosuppression Infections Infectious bursal disease Medicine and Health Sciences Physiological aspects Poultry Proteasomes Proteins Replication Research and analysis methods RNA polymerase RNA virus infections RNA viruses Standard deviation Ubiquitin-proteasome system Ubiquitination Viral infections Viral proteins Viruses VP3 protein |
| title | TRIM25 inhibits infectious bursal disease virus replication by targeting VP3 for ubiquitination and degradation |
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