Characterization and interactome study of white spot syndrome virus envelope protein VP11
White spot syndrome virus (WSSV) is a large enveloped virus. The WSSV viral particle consists of three structural layers that surround its core DNA: an outer envelope, a tegument and a nucleocapsid. Here we characterize the WSSV structural protein VP11 (WSSV394, GenBank accession number AF440570), a...
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creator | Liu, Wang-Jing Shiung, Hui-Jui Lo, Chu-Fang Leu, Jiann-Horng Lai, Ying-Jang Lee, Tai-Lin Huang, Wei-Tung Kou, Guang-Hsiung Chang, Yun-Shiang |
description | White spot syndrome virus (WSSV) is a large enveloped virus. The WSSV viral particle consists of three structural layers that surround its core DNA: an outer envelope, a tegument and a nucleocapsid. Here we characterize the WSSV structural protein VP11 (WSSV394, GenBank accession number AF440570), and use an interactome approach to analyze the possible associations between this protein and an array of other WSSV and host proteins. Temporal transcription analysis showed that vp11 is an early gene. Western blot hybridization of the intact viral particles and fractionation of the viral components, and immunoelectron microscopy showed that VP11 is an envelope protein. Membrane topology software predicted VP11 to be a type of transmembrane protein with a highly hydrophobic transmembrane domain at its N-terminal. Based on an immunofluorescence assay performed on VP11-transfected Sf9 cells and a trypsin digestion analysis of the virion, we conclude that, contrary to topology software prediction, the C-terminal of this protein is in fact inside the virion. Yeast two-hybrid screening combined with co-immunoprecipitation assays found that VP11 directly interacted with at least 12 other WSSV structural proteins as well as itself. An oligomerization assay further showed that VP11 could form dimers. VP11 is also the first reported WSSV structural protein to interact with the major nucleocapsid protein VP664. |
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The WSSV viral particle consists of three structural layers that surround its core DNA: an outer envelope, a tegument and a nucleocapsid. Here we characterize the WSSV structural protein VP11 (WSSV394, GenBank accession number AF440570), and use an interactome approach to analyze the possible associations between this protein and an array of other WSSV and host proteins. Temporal transcription analysis showed that vp11 is an early gene. Western blot hybridization of the intact viral particles and fractionation of the viral components, and immunoelectron microscopy showed that VP11 is an envelope protein. Membrane topology software predicted VP11 to be a type of transmembrane protein with a highly hydrophobic transmembrane domain at its N-terminal. Based on an immunofluorescence assay performed on VP11-transfected Sf9 cells and a trypsin digestion analysis of the virion, we conclude that, contrary to topology software prediction, the C-terminal of this protein is in fact inside the virion. Yeast two-hybrid screening combined with co-immunoprecipitation assays found that VP11 directly interacted with at least 12 other WSSV structural proteins as well as itself. An oligomerization assay further showed that VP11 could form dimers. VP11 is also the first reported WSSV structural protein to interact with the major nucleocapsid protein VP664.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0085779</identifier><identifier>PMID: 24465701</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Agriculture ; Analysis ; Assaying ; Biology ; Biotechnology ; Deoxyribonucleic acid ; Dimers ; DNA ; Fractionation ; Gene Expression Regulation, Viral ; Genes ; Herpes viruses ; Hybridization ; Hydrophobicity ; Immunoelectron microscopy ; Immunofluorescence ; Immunoprecipitation ; Infections ; Medical research ; Medical screening ; Membrane proteins ; Microscopy ; Molecular Sequence Data ; Nucleocapsids ; Oligomerization ; Penaeus monodon ; Predictions ; Protein arrays ; Protein Binding ; Protein Multimerization ; Proteins ; Reproducibility of Results ; Shellfish ; Structural proteins ; Tegument ; Time Factors ; Topology ; Transcription ; Transcription (Genetics) ; Transcription, Genetic ; Trypsin ; Two-Hybrid System Techniques ; Viral envelope proteins ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - metabolism ; Viral Envelope Proteins - ultrastructure ; Virion - metabolism ; Virions ; Virology ; Viruses ; White spot syndrome ; White spot syndrome virus 1 - genetics ; White spot syndrome virus 1 - metabolism ; White spot syndrome virus 1 - ultrastructure ; Yeast</subject><ispartof>PloS one, 2014-01, Vol.9 (1), p.e85779-e85779</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Liu 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>2014 Liu et al 2014 Liu et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-398f94198177cd47d0b45bcc5cac36956518acde8886dc95224e20abc17c95343</citedby><cites>FETCH-LOGICAL-c692t-398f94198177cd47d0b45bcc5cac36956518acde8886dc95224e20abc17c95343</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897518/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3897518/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24465701$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Söderhäll, Irene</contributor><creatorcontrib>Liu, Wang-Jing</creatorcontrib><creatorcontrib>Shiung, Hui-Jui</creatorcontrib><creatorcontrib>Lo, Chu-Fang</creatorcontrib><creatorcontrib>Leu, Jiann-Horng</creatorcontrib><creatorcontrib>Lai, Ying-Jang</creatorcontrib><creatorcontrib>Lee, Tai-Lin</creatorcontrib><creatorcontrib>Huang, Wei-Tung</creatorcontrib><creatorcontrib>Kou, Guang-Hsiung</creatorcontrib><creatorcontrib>Chang, Yun-Shiang</creatorcontrib><title>Characterization and interactome study of white spot syndrome virus envelope protein VP11</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>White spot syndrome virus (WSSV) is a large enveloped virus. The WSSV viral particle consists of three structural layers that surround its core DNA: an outer envelope, a tegument and a nucleocapsid. Here we characterize the WSSV structural protein VP11 (WSSV394, GenBank accession number AF440570), and use an interactome approach to analyze the possible associations between this protein and an array of other WSSV and host proteins. Temporal transcription analysis showed that vp11 is an early gene. Western blot hybridization of the intact viral particles and fractionation of the viral components, and immunoelectron microscopy showed that VP11 is an envelope protein. Membrane topology software predicted VP11 to be a type of transmembrane protein with a highly hydrophobic transmembrane domain at its N-terminal. Based on an immunofluorescence assay performed on VP11-transfected Sf9 cells and a trypsin digestion analysis of the virion, we conclude that, contrary to topology software prediction, the C-terminal of this protein is in fact inside the virion. Yeast two-hybrid screening combined with co-immunoprecipitation assays found that VP11 directly interacted with at least 12 other WSSV structural proteins as well as itself. An oligomerization assay further showed that VP11 could form dimers. VP11 is also the first reported WSSV structural protein to interact with the major nucleocapsid protein VP664.</description><subject>Agriculture</subject><subject>Analysis</subject><subject>Assaying</subject><subject>Biology</subject><subject>Biotechnology</subject><subject>Deoxyribonucleic acid</subject><subject>Dimers</subject><subject>DNA</subject><subject>Fractionation</subject><subject>Gene Expression Regulation, Viral</subject><subject>Genes</subject><subject>Herpes viruses</subject><subject>Hybridization</subject><subject>Hydrophobicity</subject><subject>Immunoelectron microscopy</subject><subject>Immunofluorescence</subject><subject>Immunoprecipitation</subject><subject>Infections</subject><subject>Medical research</subject><subject>Medical screening</subject><subject>Membrane proteins</subject><subject>Microscopy</subject><subject>Molecular Sequence Data</subject><subject>Nucleocapsids</subject><subject>Oligomerization</subject><subject>Penaeus monodon</subject><subject>Predictions</subject><subject>Protein arrays</subject><subject>Protein Binding</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Reproducibility of Results</subject><subject>Shellfish</subject><subject>Structural proteins</subject><subject>Tegument</subject><subject>Time Factors</subject><subject>Topology</subject><subject>Transcription</subject><subject>Transcription (Genetics)</subject><subject>Transcription, Genetic</subject><subject>Trypsin</subject><subject>Two-Hybrid System Techniques</subject><subject>Viral envelope proteins</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Viral Envelope Proteins - ultrastructure</subject><subject>Virion - metabolism</subject><subject>Virions</subject><subject>Virology</subject><subject>Viruses</subject><subject>White spot syndrome</subject><subject>White spot syndrome virus 1 - genetics</subject><subject>White spot syndrome virus 1 - metabolism</subject><subject>White spot syndrome virus 1 - 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and interactome study of white spot syndrome virus envelope protein VP11</title><author>Liu, Wang-Jing ; Shiung, Hui-Jui ; Lo, Chu-Fang ; Leu, Jiann-Horng ; Lai, Ying-Jang ; Lee, Tai-Lin ; Huang, Wei-Tung ; Kou, Guang-Hsiung ; Chang, Yun-Shiang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-398f94198177cd47d0b45bcc5cac36956518acde8886dc95224e20abc17c95343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Agriculture</topic><topic>Analysis</topic><topic>Assaying</topic><topic>Biology</topic><topic>Biotechnology</topic><topic>Deoxyribonucleic acid</topic><topic>Dimers</topic><topic>DNA</topic><topic>Fractionation</topic><topic>Gene Expression Regulation, Viral</topic><topic>Genes</topic><topic>Herpes viruses</topic><topic>Hybridization</topic><topic>Hydrophobicity</topic><topic>Immunoelectron microscopy</topic><topic>Immunofluorescence</topic><topic>Immunoprecipitation</topic><topic>Infections</topic><topic>Medical research</topic><topic>Medical screening</topic><topic>Membrane proteins</topic><topic>Microscopy</topic><topic>Molecular Sequence Data</topic><topic>Nucleocapsids</topic><topic>Oligomerization</topic><topic>Penaeus monodon</topic><topic>Predictions</topic><topic>Protein arrays</topic><topic>Protein Binding</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Reproducibility of Results</topic><topic>Shellfish</topic><topic>Structural proteins</topic><topic>Tegument</topic><topic>Time Factors</topic><topic>Topology</topic><topic>Transcription</topic><topic>Transcription (Genetics)</topic><topic>Transcription, Genetic</topic><topic>Trypsin</topic><topic>Two-Hybrid System Techniques</topic><topic>Viral envelope proteins</topic><topic>Viral Envelope Proteins - chemistry</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral 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interactome study of white spot syndrome virus envelope protein VP11</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2014-01-21</date><risdate>2014</risdate><volume>9</volume><issue>1</issue><spage>e85779</spage><epage>e85779</epage><pages>e85779-e85779</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>White spot syndrome virus (WSSV) is a large enveloped virus. The WSSV viral particle consists of three structural layers that surround its core DNA: an outer envelope, a tegument and a nucleocapsid. Here we characterize the WSSV structural protein VP11 (WSSV394, GenBank accession number AF440570), and use an interactome approach to analyze the possible associations between this protein and an array of other WSSV and host proteins. Temporal transcription analysis showed that vp11 is an early gene. Western blot hybridization of the intact viral particles and fractionation of the viral components, and immunoelectron microscopy showed that VP11 is an envelope protein. Membrane topology software predicted VP11 to be a type of transmembrane protein with a highly hydrophobic transmembrane domain at its N-terminal. Based on an immunofluorescence assay performed on VP11-transfected Sf9 cells and a trypsin digestion analysis of the virion, we conclude that, contrary to topology software prediction, the C-terminal of this protein is in fact inside the virion. Yeast two-hybrid screening combined with co-immunoprecipitation assays found that VP11 directly interacted with at least 12 other WSSV structural proteins as well as itself. An oligomerization assay further showed that VP11 could form dimers. VP11 is also the first reported WSSV structural protein to interact with the major nucleocapsid protein VP664.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24465701</pmid><doi>10.1371/journal.pone.0085779</doi><tpages>e85779</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Agriculture Analysis Assaying Biology Biotechnology Deoxyribonucleic acid Dimers DNA Fractionation Gene Expression Regulation, Viral Genes Herpes viruses Hybridization Hydrophobicity Immunoelectron microscopy Immunofluorescence Immunoprecipitation Infections Medical research Medical screening Membrane proteins Microscopy Molecular Sequence Data Nucleocapsids Oligomerization Penaeus monodon Predictions Protein arrays Protein Binding Protein Multimerization Proteins Reproducibility of Results Shellfish Structural proteins Tegument Time Factors Topology Transcription Transcription (Genetics) Transcription, Genetic Trypsin Two-Hybrid System Techniques Viral envelope proteins Viral Envelope Proteins - chemistry Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Viral Envelope Proteins - ultrastructure Virion - metabolism Virions Virology Viruses White spot syndrome White spot syndrome virus 1 - genetics White spot syndrome virus 1 - metabolism White spot syndrome virus 1 - ultrastructure Yeast |
title | Characterization and interactome study of white spot syndrome virus envelope protein VP11 |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T17%3A21%3A33IST&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=Characterization%20and%20interactome%20study%20of%20white%20spot%20syndrome%20virus%20envelope%20protein%20VP11&rft.jtitle=PloS%20one&rft.au=Liu,%20Wang-Jing&rft.date=2014-01-21&rft.volume=9&rft.issue=1&rft.spage=e85779&rft.epage=e85779&rft.pages=e85779-e85779&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0085779&rft_dat=%3Cgale_plos_%3EA478855616%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=1490992850&rft_id=info:pmid/24465701&rft_galeid=A478855616&rft_doaj_id=oai_doaj_org_article_f5a620d467924b7b97333b5f3850537c&rfr_iscdi=true |