The interaction between endogenous 30S ribosomal subunit protein S11 and Cucumber mosaic virus LS2b protein affects viral replication, infection and gene silencing suppressor activity
Cucumber mosaic virus (CMV) is a model virus for plant-virus protein interaction and mechanism research because of its wide distribution, high-level of replication and simple genome structure. The 2b protein is a multifunctional protein encoded by CMV that suppresses RNA silencing-based antiviral de...
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| description | Cucumber mosaic virus (CMV) is a model virus for plant-virus protein interaction and mechanism research because of its wide distribution, high-level of replication and simple genome structure. The 2b protein is a multifunctional protein encoded by CMV that suppresses RNA silencing-based antiviral defense and contributes to CMV virulence in host plants. In this report, 12 host proteins were identified as CMV LS2b binding partners using the yeast two-hybrid screen system from the Arabidopsis thaliana cDNA library. Among the host proteins, 30S ribosomal subunit protein S11 (RPS11) was selected for further studies. The interaction between LS2b and full-length RPS11 was confirmed using the yeast two-hybrid system. Bimolecular fluorescence complementation (BIFC) assays observed by confocal laser microscopy and Glutathione S-transferase (GST) pull-down assays were used to verify the interaction between endogenous NbRPS11 and viral CMVLS2b both in vivo and in vitro. TRV-based gene silencing vector was used to knockdown NbRPS11 transcription, and immunoblot analysis revealed a decline in infectious viral RNA replication and a decrease in CMV infection in RPS11 down-regulated Nicotiana benthamiana plants. Thus, the knockdown of RPS11 likely inhibited CMV replication and accumulation. The gene silencing suppressor activity of CMV2b protein was reduced by the RPS11 knockdown. This study demonstrated that the function of viral LS2b protein was remarkably affected by the interaction with host RPS11 protein. |
| doi_str_mv | 10.1371/journal.pone.0182459 |
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The 2b protein is a multifunctional protein encoded by CMV that suppresses RNA silencing-based antiviral defense and contributes to CMV virulence in host plants. In this report, 12 host proteins were identified as CMV LS2b binding partners using the yeast two-hybrid screen system from the Arabidopsis thaliana cDNA library. Among the host proteins, 30S ribosomal subunit protein S11 (RPS11) was selected for further studies. The interaction between LS2b and full-length RPS11 was confirmed using the yeast two-hybrid system. Bimolecular fluorescence complementation (BIFC) assays observed by confocal laser microscopy and Glutathione S-transferase (GST) pull-down assays were used to verify the interaction between endogenous NbRPS11 and viral CMVLS2b both in vivo and in vitro. TRV-based gene silencing vector was used to knockdown NbRPS11 transcription, and immunoblot analysis revealed a decline in infectious viral RNA replication and a decrease in CMV infection in RPS11 down-regulated Nicotiana benthamiana plants. Thus, the knockdown of RPS11 likely inhibited CMV replication and accumulation. The gene silencing suppressor activity of CMV2b protein was reduced by the RPS11 knockdown. This study demonstrated that the function of viral LS2b protein was remarkably affected by the interaction with host RPS11 protein.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0182459</identifier><identifier>PMID: 28806733</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Arabidopsis - metabolism ; Arabidopsis - virology ; Arabidopsis thaliana ; Beans ; Biology and Life Sciences ; Complementation ; Cucumovirus - physiology ; Fluorescence ; Gene Knockdown Techniques ; Gene Silencing ; Genes ; Genomes ; Glutathione ; Glutathione transferase ; Host plants ; Hybrid systems ; In vitro methods and tests ; Infections ; Laser microscopy ; Laser scanning microscopy ; Life sciences ; Medical screening ; Medicine and Health Sciences ; Microscopy ; Nicotiana - metabolism ; Nicotiana - virology ; Plant Diseases - virology ; Plant Proteins - metabolism ; Plant virus diseases ; Plant viruses ; Protein Binding ; Protein structure ; Protein synthesis ; Proteins ; Replication ; Reproducibility of Results ; Research and Analysis Methods ; Ribonucleic acid ; Ribosomal Proteins - metabolism ; RNA ; RNA, Viral - metabolism ; RNA-mediated interference ; Studies ; Tobacco ; Transcription ; Transcription (Genetics) ; Two-Hybrid System Techniques ; Viral infections ; Viral Proteins - metabolism ; Virion - metabolism ; Virulence ; Virus Replication - physiology ; Viruses ; Yeast ; Yeasts</subject><ispartof>PloS one, 2017-08, Vol.12 (8), p.e0182459-e0182459</ispartof><rights>COPYRIGHT 2017 Public Library of Science</rights><rights>2017 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>2017 Wang et al 2017 Wang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-c9d9b6bfffb590abe8aaf0e69b149d3dc46bc2cf3c0b01ed2a8dd364ff5487d53</citedby><cites>FETCH-LOGICAL-c692t-c9d9b6bfffb590abe8aaf0e69b149d3dc46bc2cf3c0b01ed2a8dd364ff5487d53</cites><orcidid>0000-0003-2288-3361</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/PMC5555695/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5555695/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2101,2927,23865,27923,27924,53790,53792,79471,79472</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28806733$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Wong, Sek-Man</contributor><creatorcontrib>Wang, Ruilin</creatorcontrib><creatorcontrib>Du, Zhiyou</creatorcontrib><creatorcontrib>Bai, Zhenqing</creatorcontrib><creatorcontrib>Liang, Zongsuo</creatorcontrib><title>The interaction between endogenous 30S ribosomal subunit protein S11 and Cucumber mosaic virus LS2b protein affects viral replication, infection and gene silencing suppressor activity</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Cucumber mosaic virus (CMV) is a model virus for plant-virus protein interaction and mechanism research because of its wide distribution, high-level of replication and simple genome structure. The 2b protein is a multifunctional protein encoded by CMV that suppresses RNA silencing-based antiviral defense and contributes to CMV virulence in host plants. In this report, 12 host proteins were identified as CMV LS2b binding partners using the yeast two-hybrid screen system from the Arabidopsis thaliana cDNA library. Among the host proteins, 30S ribosomal subunit protein S11 (RPS11) was selected for further studies. The interaction between LS2b and full-length RPS11 was confirmed using the yeast two-hybrid system. Bimolecular fluorescence complementation (BIFC) assays observed by confocal laser microscopy and Glutathione S-transferase (GST) pull-down assays were used to verify the interaction between endogenous NbRPS11 and viral CMVLS2b both in vivo and in vitro. TRV-based gene silencing vector was used to knockdown NbRPS11 transcription, and immunoblot analysis revealed a decline in infectious viral RNA replication and a decrease in CMV infection in RPS11 down-regulated Nicotiana benthamiana plants. Thus, the knockdown of RPS11 likely inhibited CMV replication and accumulation. The gene silencing suppressor activity of CMV2b protein was reduced by the RPS11 knockdown. This study demonstrated that the function of viral LS2b protein was remarkably affected by the interaction with host RPS11 protein.</description><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - virology</subject><subject>Arabidopsis thaliana</subject><subject>Beans</subject><subject>Biology and Life Sciences</subject><subject>Complementation</subject><subject>Cucumovirus - physiology</subject><subject>Fluorescence</subject><subject>Gene Knockdown Techniques</subject><subject>Gene Silencing</subject><subject>Genes</subject><subject>Genomes</subject><subject>Glutathione</subject><subject>Glutathione transferase</subject><subject>Host plants</subject><subject>Hybrid systems</subject><subject>In vitro methods and tests</subject><subject>Infections</subject><subject>Laser microscopy</subject><subject>Laser scanning microscopy</subject><subject>Life sciences</subject><subject>Medical screening</subject><subject>Medicine and Health Sciences</subject><subject>Microscopy</subject><subject>Nicotiana - metabolism</subject><subject>Nicotiana - virology</subject><subject>Plant Diseases - virology</subject><subject>Plant Proteins - metabolism</subject><subject>Plant virus diseases</subject><subject>Plant viruses</subject><subject>Protein Binding</subject><subject>Protein structure</subject><subject>Protein synthesis</subject><subject>Proteins</subject><subject>Replication</subject><subject>Reproducibility of Results</subject><subject>Research and Analysis Methods</subject><subject>Ribonucleic acid</subject><subject>Ribosomal Proteins - metabolism</subject><subject>RNA</subject><subject>RNA, Viral - metabolism</subject><subject>RNA-mediated interference</subject><subject>Studies</subject><subject>Tobacco</subject><subject>Transcription</subject><subject>Transcription (Genetics)</subject><subject>Two-Hybrid System Techniques</subject><subject>Viral infections</subject><subject>Viral Proteins - metabolism</subject><subject>Virion - metabolism</subject><subject>Virulence</subject><subject>Virus Replication - 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metabolism</topic><topic>Arabidopsis - virology</topic><topic>Arabidopsis thaliana</topic><topic>Beans</topic><topic>Biology and Life Sciences</topic><topic>Complementation</topic><topic>Cucumovirus - physiology</topic><topic>Fluorescence</topic><topic>Gene Knockdown Techniques</topic><topic>Gene Silencing</topic><topic>Genes</topic><topic>Genomes</topic><topic>Glutathione</topic><topic>Glutathione transferase</topic><topic>Host plants</topic><topic>Hybrid systems</topic><topic>In vitro methods and tests</topic><topic>Infections</topic><topic>Laser microscopy</topic><topic>Laser scanning microscopy</topic><topic>Life sciences</topic><topic>Medical screening</topic><topic>Medicine and Health Sciences</topic><topic>Microscopy</topic><topic>Nicotiana - metabolism</topic><topic>Nicotiana - virology</topic><topic>Plant Diseases - virology</topic><topic>Plant Proteins - metabolism</topic><topic>Plant virus diseases</topic><topic>Plant viruses</topic><topic>Protein Binding</topic><topic>Protein structure</topic><topic>Protein synthesis</topic><topic>Proteins</topic><topic>Replication</topic><topic>Reproducibility of Results</topic><topic>Research and Analysis Methods</topic><topic>Ribonucleic acid</topic><topic>Ribosomal Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Ruilin</au><au>Du, Zhiyou</au><au>Bai, Zhenqing</au><au>Liang, Zongsuo</au><au>Wong, Sek-Man</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The interaction between endogenous 30S ribosomal subunit protein S11 and Cucumber mosaic virus LS2b protein affects viral replication, infection and gene silencing suppressor activity</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2017-08-14</date><risdate>2017</risdate><volume>12</volume><issue>8</issue><spage>e0182459</spage><epage>e0182459</epage><pages>e0182459-e0182459</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Cucumber mosaic virus (CMV) is a model virus for plant-virus protein interaction and mechanism research because of its wide distribution, high-level of replication and simple genome structure. The 2b protein is a multifunctional protein encoded by CMV that suppresses RNA silencing-based antiviral defense and contributes to CMV virulence in host plants. In this report, 12 host proteins were identified as CMV LS2b binding partners using the yeast two-hybrid screen system from the Arabidopsis thaliana cDNA library. Among the host proteins, 30S ribosomal subunit protein S11 (RPS11) was selected for further studies. The interaction between LS2b and full-length RPS11 was confirmed using the yeast two-hybrid system. Bimolecular fluorescence complementation (BIFC) assays observed by confocal laser microscopy and Glutathione S-transferase (GST) pull-down assays were used to verify the interaction between endogenous NbRPS11 and viral CMVLS2b both in vivo and in vitro. TRV-based gene silencing vector was used to knockdown NbRPS11 transcription, and immunoblot analysis revealed a decline in infectious viral RNA replication and a decrease in CMV infection in RPS11 down-regulated Nicotiana benthamiana plants. Thus, the knockdown of RPS11 likely inhibited CMV replication and accumulation. The gene silencing suppressor activity of CMV2b protein was reduced by the RPS11 knockdown. This study demonstrated that the function of viral LS2b protein was remarkably affected by the interaction with host RPS11 protein.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>28806733</pmid><doi>10.1371/journal.pone.0182459</doi><tpages>e0182459</tpages><orcidid>https://orcid.org/0000-0003-2288-3361</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS); EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Arabidopsis - metabolism Arabidopsis - virology Arabidopsis thaliana Beans Biology and Life Sciences Complementation Cucumovirus - physiology Fluorescence Gene Knockdown Techniques Gene Silencing Genes Genomes Glutathione Glutathione transferase Host plants Hybrid systems In vitro methods and tests Infections Laser microscopy Laser scanning microscopy Life sciences Medical screening Medicine and Health Sciences Microscopy Nicotiana - metabolism Nicotiana - virology Plant Diseases - virology Plant Proteins - metabolism Plant virus diseases Plant viruses Protein Binding Protein structure Protein synthesis Proteins Replication Reproducibility of Results Research and Analysis Methods Ribonucleic acid Ribosomal Proteins - metabolism RNA RNA, Viral - metabolism RNA-mediated interference Studies Tobacco Transcription Transcription (Genetics) Two-Hybrid System Techniques Viral infections Viral Proteins - metabolism Virion - metabolism Virulence Virus Replication - physiology Viruses Yeast Yeasts |
| title | The interaction between endogenous 30S ribosomal subunit protein S11 and Cucumber mosaic virus LS2b protein affects viral replication, infection and gene silencing suppressor activity |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T19%3A37%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20interaction%20between%20endogenous%2030S%20ribosomal%20subunit%20protein%20S11%20and%20Cucumber%20mosaic%20virus%20LS2b%20protein%20affects%20viral%20replication,%20infection%20and%20gene%20silencing%20suppressor%20activity&rft.jtitle=PloS%20one&rft.au=Wang,%20Ruilin&rft.date=2017-08-14&rft.volume=12&rft.issue=8&rft.spage=e0182459&rft.epage=e0182459&rft.pages=e0182459-e0182459&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0182459&rft_dat=%3Cgale_plos_%3EA500574550%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1928765638&rft_id=info:pmid/28806733&rft_galeid=A500574550&rft_doaj_id=oai_doaj_org_article_06d623a0e9fb4714b938c4f1ceade120&rfr_iscdi=true |