Oligomerization of Baculovirus LEF-11 Is Involved in Viral DNA Replication
We have previously reported that baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) late expression factor 11 (lef-11) is associated with viral DNA replication and have demonstrated that it potentially interacts with itself; however, whether LEF-11 forms oligomers and the impact of LEF-11 oligomer...
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| creator | Dong, Zhan-Qi Hu, Nan Zhang, Jun Chen, Ting-Ting Cao, Ming-Ya Li, Hai-Qing Lei, Xue-Jiao Chen, Peng Lu, Cheng Pan, Min-Hui |
| description | We have previously reported that baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) late expression factor 11 (lef-11) is associated with viral DNA replication and have demonstrated that it potentially interacts with itself; however, whether LEF-11 forms oligomers and the impact of LEF-11 oligomerization on viral function have not been substantiated. In this study, we first demonstrated that LEF-11 is capable of forming oligomers. Additionally, a series of analyses using BmNPV LEF-11 truncation mutants indicated that two distinct domains control LEF-11 oligomerization (aa 42-61 and aa 72-101). LEF-11 truncation constructs were inserted into a lef-11-knockout BmNPV bacmid, which was used to demonstrate that truncated LEF-11 lacking either oligomerization domain abrogates viral DNA replication. Finally, site-directed mutagenesis was used to determine that the conserved hydrophobic residues Y58&I59 (representing Y58 and I59), I85 and L88&L89 (representing L88 and L89) are required for LEF-11 oligomerization and viral DNA replication. Collectively, these data indicate that BmNPV LEF-11 oligomerization influences viral DNA replication. |
| doi_str_mv | 10.1371/journal.pone.0144930 |
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In this study, we first demonstrated that LEF-11 is capable of forming oligomers. Additionally, a series of analyses using BmNPV LEF-11 truncation mutants indicated that two distinct domains control LEF-11 oligomerization (aa 42-61 and aa 72-101). LEF-11 truncation constructs were inserted into a lef-11-knockout BmNPV bacmid, which was used to demonstrate that truncated LEF-11 lacking either oligomerization domain abrogates viral DNA replication. Finally, site-directed mutagenesis was used to determine that the conserved hydrophobic residues Y58&I59 (representing Y58 and I59), I85 and L88&L89 (representing L88 and L89) are required for LEF-11 oligomerization and viral DNA replication. Collectively, these data indicate that BmNPV LEF-11 oligomerization influences viral DNA replication.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0144930</identifier><identifier>PMID: 26660313</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Analysis ; Animals ; Baculovirus ; Bombyx - virology ; Bombyx mori ; Cell Line ; Deoxyribonucleic acid ; DNA ; DNA biosynthesis ; DNA replication ; DNA, Viral - metabolism ; Gene expression ; Gene Knockout Techniques ; Genetic Vectors - genetics ; Genetic Vectors - metabolism ; Genomics ; Hydrophobicity ; Laboratories ; Microscopy, Fluorescence ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutants ; Nucleopolyhedrovirus - genetics ; Nucleopolyhedrovirus - physiology ; Oligomerization ; Oligomers ; Plasmids ; Protein Multimerization ; Real-Time Polymerase Chain Reaction ; Replication ; Site-directed mutagenesis ; Viral Proteins - chemistry ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Virus Replication ; Viruses</subject><ispartof>PloS one, 2015-12, Vol.10 (12), p.e0144930</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Dong 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>2015 Dong et al 2015 Dong et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c762t-bdb70d8cf3a91096d4ee6f58d915b7e65eb29565becac6c03edb0a2e1a101a023</citedby><cites>FETCH-LOGICAL-c762t-bdb70d8cf3a91096d4ee6f58d915b7e65eb29565becac6c03edb0a2e1a101a023</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/PMC4678028/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4678028/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53770,53772,79347,79348</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26660313$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Lopez-Ferber, Miguel</contributor><creatorcontrib>Dong, Zhan-Qi</creatorcontrib><creatorcontrib>Hu, Nan</creatorcontrib><creatorcontrib>Zhang, Jun</creatorcontrib><creatorcontrib>Chen, Ting-Ting</creatorcontrib><creatorcontrib>Cao, Ming-Ya</creatorcontrib><creatorcontrib>Li, Hai-Qing</creatorcontrib><creatorcontrib>Lei, Xue-Jiao</creatorcontrib><creatorcontrib>Chen, Peng</creatorcontrib><creatorcontrib>Lu, Cheng</creatorcontrib><creatorcontrib>Pan, Min-Hui</creatorcontrib><title>Oligomerization of Baculovirus LEF-11 Is Involved in Viral DNA Replication</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>We have previously reported that baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) late expression factor 11 (lef-11) is associated with viral DNA replication and have demonstrated that it potentially interacts with itself; however, whether LEF-11 forms oligomers and the impact of LEF-11 oligomerization on viral function have not been substantiated. In this study, we first demonstrated that LEF-11 is capable of forming oligomers. Additionally, a series of analyses using BmNPV LEF-11 truncation mutants indicated that two distinct domains control LEF-11 oligomerization (aa 42-61 and aa 72-101). LEF-11 truncation constructs were inserted into a lef-11-knockout BmNPV bacmid, which was used to demonstrate that truncated LEF-11 lacking either oligomerization domain abrogates viral DNA replication. Finally, site-directed mutagenesis was used to determine that the conserved hydrophobic residues Y58&I59 (representing Y58 and I59), I85 and L88&L89 (representing L88 and L89) are required for LEF-11 oligomerization and viral DNA replication. Collectively, these data indicate that BmNPV LEF-11 oligomerization influences viral DNA replication.</description><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Animals</subject><subject>Baculovirus</subject><subject>Bombyx - virology</subject><subject>Bombyx mori</subject><subject>Cell Line</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA biosynthesis</subject><subject>DNA replication</subject><subject>DNA, Viral - metabolism</subject><subject>Gene expression</subject><subject>Gene Knockout Techniques</subject><subject>Genetic Vectors - genetics</subject><subject>Genetic Vectors - metabolism</subject><subject>Genomics</subject><subject>Hydrophobicity</subject><subject>Laboratories</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutants</subject><subject>Nucleopolyhedrovirus - genetics</subject><subject>Nucleopolyhedrovirus - physiology</subject><subject>Oligomerization</subject><subject>Oligomers</subject><subject>Plasmids</subject><subject>Protein Multimerization</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Replication</subject><subject>Site-directed mutagenesis</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Replication</subject><subject>Viruses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><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>eNqNkl2L1DAUhoso7rr6D0QLguBFx3w1bW-EcT-0Mjiw6t6GND3tZMg0Y9IOq7_ezE53mYKC5CLh5HnfJCdvFL3EaIZpht-v7eA6aWZb28EMYcYKih5Fp7igJOEE0cdH65PomfdrhFKac_40OiGcc0QxPY2-LI1u7Qac_i17bbvYNvFHqQZjd9oNPl5cXiUYx6WPy25nzQ7qWHfxjXbSxBdf5_E1bI1Wd9Ln0ZNGGg8vxvks-nF1-f38c7JYfirP54tEZZz0SVVXGapz1VBZYFTwmgHwJs3rAqdVBjyFihQpTytQUnGFKNQVkgSwxAhLROhZ9PrguzXWi7ENXuCM5XmaY5wFojwQtZVrsXV6I90vYaUWdwXrWiFdr5UBoTAlTV7JtGo4I4WSTYFxWsiCVEzlAMHrw3jaUG2gVtD14e0T0-lOp1eitTvBeJYjkgeDN6OBsz8H8P0_rjxSrQy30l1jg5naaK_EnNGMhf9iKFCzv1Bh1LDRKgSh0aE-EbybCALTw23fysF7UX67_n92eTNl3x6xK5CmX3lrhn0O_BRkB1A5672D5qFzGIl9ju-7IfY5FmOOg-zVcdcfRPfBpX8AzWHsmg</recordid><startdate>20151214</startdate><enddate>20151214</enddate><creator>Dong, Zhan-Qi</creator><creator>Hu, Nan</creator><creator>Zhang, Jun</creator><creator>Chen, Ting-Ting</creator><creator>Cao, Ming-Ya</creator><creator>Li, Hai-Qing</creator><creator>Lei, Xue-Jiao</creator><creator>Chen, Peng</creator><creator>Lu, Cheng</creator><creator>Pan, Min-Hui</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20151214</creationdate><title>Oligomerization of Baculovirus LEF-11 Is Involved in Viral DNA Replication</title><author>Dong, Zhan-Qi ; Hu, Nan ; Zhang, Jun ; Chen, Ting-Ting ; Cao, Ming-Ya ; Li, Hai-Qing ; Lei, Xue-Jiao ; Chen, Peng ; Lu, Cheng ; Pan, Min-Hui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c762t-bdb70d8cf3a91096d4ee6f58d915b7e65eb29565becac6c03edb0a2e1a101a023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acid Sequence</topic><topic>Analysis</topic><topic>Animals</topic><topic>Baculovirus</topic><topic>Bombyx - virology</topic><topic>Bombyx mori</topic><topic>Cell Line</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA biosynthesis</topic><topic>DNA replication</topic><topic>DNA, Viral - metabolism</topic><topic>Gene expression</topic><topic>Gene Knockout Techniques</topic><topic>Genetic Vectors - genetics</topic><topic>Genetic Vectors - metabolism</topic><topic>Genomics</topic><topic>Hydrophobicity</topic><topic>Laboratories</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutants</topic><topic>Nucleopolyhedrovirus - genetics</topic><topic>Nucleopolyhedrovirus - physiology</topic><topic>Oligomerization</topic><topic>Oligomers</topic><topic>Plasmids</topic><topic>Protein Multimerization</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Replication</topic><topic>Site-directed mutagenesis</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - 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In this study, we first demonstrated that LEF-11 is capable of forming oligomers. Additionally, a series of analyses using BmNPV LEF-11 truncation mutants indicated that two distinct domains control LEF-11 oligomerization (aa 42-61 and aa 72-101). LEF-11 truncation constructs were inserted into a lef-11-knockout BmNPV bacmid, which was used to demonstrate that truncated LEF-11 lacking either oligomerization domain abrogates viral DNA replication. Finally, site-directed mutagenesis was used to determine that the conserved hydrophobic residues Y58&I59 (representing Y58 and I59), I85 and L88&L89 (representing L88 and L89) are required for LEF-11 oligomerization and viral DNA replication. Collectively, these data indicate that BmNPV LEF-11 oligomerization influences viral DNA replication.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26660313</pmid><doi>10.1371/journal.pone.0144930</doi><tpages>e0144930</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Analysis Animals Baculovirus Bombyx - virology Bombyx mori Cell Line Deoxyribonucleic acid DNA DNA biosynthesis DNA replication DNA, Viral - metabolism Gene expression Gene Knockout Techniques Genetic Vectors - genetics Genetic Vectors - metabolism Genomics Hydrophobicity Laboratories Microscopy, Fluorescence Molecular Sequence Data Mutagenesis, Site-Directed Mutants Nucleopolyhedrovirus - genetics Nucleopolyhedrovirus - physiology Oligomerization Oligomers Plasmids Protein Multimerization Real-Time Polymerase Chain Reaction Replication Site-directed mutagenesis Viral Proteins - chemistry Viral Proteins - genetics Viral Proteins - metabolism Virus Replication Viruses |
| title | Oligomerization of Baculovirus LEF-11 Is Involved in Viral DNA Replication |
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