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Nonvirus encoded proteins could be embedded into Bombyx mori cypovirus polyhedra
To explore whether the nonvirus encoded protein could be embedded into Bombyx mori cypovirus (BmCPV) polyhedra. The stable transformants of BmN cells expressing a polyhedrin (Polh) gene of BmCPV were constructed by transfection with a non-transposon derived vector containing a polh gene. The polyhed...
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Published in: | Molecular biology reports 2014, Vol.41 (4), p.2657-2666 |
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description | To explore whether the nonvirus encoded protein could be embedded into Bombyx mori cypovirus (BmCPV) polyhedra. The stable transformants of BmN cells expressing a polyhedrin (Polh) gene of BmCPV were constructed by transfection with a non-transposon derived vector containing a polh gene. The polyhedra were purified from the midguts of BmCPV-infected silkworms and the transformed BmN cells, respectively. The proteins embedded into polyhedra were determined by mass spectrometry analysis. Host derived proteins were detected in the purified polyhedra. Analysis of structure and hydrophilicity of embedded proteins indicated that the hydrophilic proteins, in structure, were similar to the left-handed structure of polyhedrin or the N-terminal domain of BmCPV structural protein VP3, which were easily embedded into the BmCPV polyhedra. The lysate of polyhedra purified from the infected transformation of BmN cells with modified B. mori baculovirus BmPAK6 could infect BmN cells, indicating that B. mori baculovirus could be embedded into BmCPV polyhedra. Both the purified polyhedra and its lysate could be coloured by X-gal, indicating that the β-galactosidase expressed by BmPAK6 could be incorporated into BmCPV polyhedra. These results suggested that some heterologous proteins and baculovirus could be embedded into polyhedra in an unknown manner. |
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The stable transformants of BmN cells expressing a polyhedrin (Polh) gene of BmCPV were constructed by transfection with a non-transposon derived vector containing a polh gene. The polyhedra were purified from the midguts of BmCPV-infected silkworms and the transformed BmN cells, respectively. The proteins embedded into polyhedra were determined by mass spectrometry analysis. Host derived proteins were detected in the purified polyhedra. Analysis of structure and hydrophilicity of embedded proteins indicated that the hydrophilic proteins, in structure, were similar to the left-handed structure of polyhedrin or the N-terminal domain of BmCPV structural protein VP3, which were easily embedded into the BmCPV polyhedra. The lysate of polyhedra purified from the infected transformation of BmN cells with modified B. mori baculovirus BmPAK6 could infect BmN cells, indicating that B. mori baculovirus could be embedded into BmCPV polyhedra. Both the purified polyhedra and its lysate could be coloured by X-gal, indicating that the β-galactosidase expressed by BmPAK6 could be incorporated into BmCPV polyhedra. These results suggested that some heterologous proteins and baculovirus could be embedded into polyhedra in an unknown manner.</description><identifier>ISSN: 0301-4851</identifier><identifier>EISSN: 1573-4978</identifier><identifier>DOI: 10.1007/s11033-014-3124-7</identifier><identifier>PMID: 24469718</identifier><language>eng</language><publisher>Dordrecht: Springer-Verlag</publisher><subject>Animal Anatomy ; Animal Biochemistry ; Animals ; Baculoviridae ; Baculoviridae - genetics ; Baculoviridae - metabolism ; beta-galactosidase ; beta-Galactosidase - genetics ; beta-Galactosidase - metabolism ; Biomedical and Life Sciences ; Bombyx - virology ; Bombyx mori ; Cell Line ; Cypovirus ; genes ; Histology ; Host-Pathogen Interactions ; hydrophilicity ; Life Sciences ; Mass spectrometry ; Models, Molecular ; Molecular biology ; Morphology ; Protein Conformation ; Proteins ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Reoviridae - physiology ; silkworms ; transfection ; Viral Structural Proteins - chemistry ; Viral Structural Proteins - metabolism ; Virus Assembly ; Viruses</subject><ispartof>Molecular biology reports, 2014, Vol.41 (4), p.2657-2666</ispartof><rights>Springer Science+Business Media Dordrecht 2014</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396t-cf719462acfbc002613296161cfc2ebffff6b3d5acf5c5d462c8ebb3fe0c14353</citedby><cites>FETCH-LOGICAL-c396t-cf719462acfbc002613296161cfc2ebffff6b3d5acf5c5d462c8ebb3fe0c14353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24469718$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Yi-ling</creatorcontrib><creatorcontrib>Xue, Ren-yu</creatorcontrib><creatorcontrib>Cao, Guang-li</creatorcontrib><creatorcontrib>Meng, Xiang-kun</creatorcontrib><creatorcontrib>Zhu, Yue-xiong</creatorcontrib><creatorcontrib>Pan, Zhong-hua</creatorcontrib><creatorcontrib>Gong, Cheng-liang</creatorcontrib><title>Nonvirus encoded proteins could be embedded into Bombyx mori cypovirus polyhedra</title><title>Molecular biology reports</title><addtitle>Mol Biol Rep</addtitle><addtitle>Mol Biol Rep</addtitle><description>To explore whether the nonvirus encoded protein could be embedded into Bombyx mori cypovirus (BmCPV) polyhedra. The stable transformants of BmN cells expressing a polyhedrin (Polh) gene of BmCPV were constructed by transfection with a non-transposon derived vector containing a polh gene. The polyhedra were purified from the midguts of BmCPV-infected silkworms and the transformed BmN cells, respectively. The proteins embedded into polyhedra were determined by mass spectrometry analysis. Host derived proteins were detected in the purified polyhedra. Analysis of structure and hydrophilicity of embedded proteins indicated that the hydrophilic proteins, in structure, were similar to the left-handed structure of polyhedrin or the N-terminal domain of BmCPV structural protein VP3, which were easily embedded into the BmCPV polyhedra. The lysate of polyhedra purified from the infected transformation of BmN cells with modified B. mori baculovirus BmPAK6 could infect BmN cells, indicating that B. mori baculovirus could be embedded into BmCPV polyhedra. Both the purified polyhedra and its lysate could be coloured by X-gal, indicating that the β-galactosidase expressed by BmPAK6 could be incorporated into BmCPV polyhedra. These results suggested that some heterologous proteins and baculovirus could be embedded into polyhedra in an unknown manner.</description><subject>Animal Anatomy</subject><subject>Animal Biochemistry</subject><subject>Animals</subject><subject>Baculoviridae</subject><subject>Baculoviridae - genetics</subject><subject>Baculoviridae - metabolism</subject><subject>beta-galactosidase</subject><subject>beta-Galactosidase - genetics</subject><subject>beta-Galactosidase - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Bombyx - virology</subject><subject>Bombyx mori</subject><subject>Cell Line</subject><subject>Cypovirus</subject><subject>genes</subject><subject>Histology</subject><subject>Host-Pathogen Interactions</subject><subject>hydrophilicity</subject><subject>Life Sciences</subject><subject>Mass spectrometry</subject><subject>Models, Molecular</subject><subject>Molecular biology</subject><subject>Morphology</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Reoviridae - physiology</subject><subject>silkworms</subject><subject>transfection</subject><subject>Viral Structural Proteins - chemistry</subject><subject>Viral Structural Proteins - metabolism</subject><subject>Virus Assembly</subject><subject>Viruses</subject><issn>0301-4851</issn><issn>1573-4978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNp9kE1P3DAQhq0KxC5bfkAvNFIvXEJnbCdOjnRVPiTUIlHOVuxMaFASb-1Nxf77OspSIQ74Mod53tejh7FPCOcIoL4GRBAiBZSpQC5T9YEtMVMilaUqDtgSBGAqiwwX7DiEJwCQqLIjtuBS5qXCYsnufrjhb-vHkNBgXU11svFuS-0QEuvGrk4MJdQbqqdVO2xd8s31Zvec9M63id1t3JzeuG73m2pffWSHTdUFOtnPFXu4_P5rfZ3e_ry6WV_cplaU-Ta1jcJS5ryyjbEAPEfByxxztI3lZJr4ciPqLO4zm9WRtAUZIxoCi1JkYsXO5t5475-Rwlb3bbDUddVAbgwaM0RRTq0R_fIGfXKjH-J1EwUqyhBFpHCmrHcheGr0xrd95XcaQU-69axbR9160q1VzJzum0fTU_0_8eI3AnwGQlwNj-Rfff1O6-c51FROV4--DfrhnkcAAAHzkot_cueUGQ</recordid><startdate>2014</startdate><enddate>2014</enddate><creator>Zhang, Yi-ling</creator><creator>Xue, Ren-yu</creator><creator>Cao, Guang-li</creator><creator>Meng, Xiang-kun</creator><creator>Zhu, Yue-xiong</creator><creator>Pan, Zhong-hua</creator><creator>Gong, Cheng-liang</creator><general>Springer-Verlag</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>FBQ</scope><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>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>2014</creationdate><title>Nonvirus encoded proteins could be embedded into Bombyx mori cypovirus polyhedra</title><author>Zhang, Yi-ling ; Xue, Ren-yu ; Cao, Guang-li ; Meng, Xiang-kun ; Zhu, Yue-xiong ; Pan, Zhong-hua ; Gong, Cheng-liang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-cf719462acfbc002613296161cfc2ebffff6b3d5acf5c5d462c8ebb3fe0c14353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Animal Anatomy</topic><topic>Animal Biochemistry</topic><topic>Animals</topic><topic>Baculoviridae</topic><topic>Baculoviridae - genetics</topic><topic>Baculoviridae - metabolism</topic><topic>beta-galactosidase</topic><topic>beta-Galactosidase - genetics</topic><topic>beta-Galactosidase - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Bombyx - virology</topic><topic>Bombyx mori</topic><topic>Cell Line</topic><topic>Cypovirus</topic><topic>genes</topic><topic>Histology</topic><topic>Host-Pathogen Interactions</topic><topic>hydrophilicity</topic><topic>Life Sciences</topic><topic>Mass spectrometry</topic><topic>Models, Molecular</topic><topic>Molecular biology</topic><topic>Morphology</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Reoviridae - physiology</topic><topic>silkworms</topic><topic>transfection</topic><topic>Viral Structural Proteins - chemistry</topic><topic>Viral Structural Proteins - metabolism</topic><topic>Virus Assembly</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Yi-ling</creatorcontrib><creatorcontrib>Xue, Ren-yu</creatorcontrib><creatorcontrib>Cao, Guang-li</creatorcontrib><creatorcontrib>Meng, Xiang-kun</creatorcontrib><creatorcontrib>Zhu, Yue-xiong</creatorcontrib><creatorcontrib>Pan, Zhong-hua</creatorcontrib><creatorcontrib>Gong, Cheng-liang</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular biology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Yi-ling</au><au>Xue, Ren-yu</au><au>Cao, Guang-li</au><au>Meng, Xiang-kun</au><au>Zhu, Yue-xiong</au><au>Pan, Zhong-hua</au><au>Gong, Cheng-liang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nonvirus encoded proteins could be embedded into Bombyx mori cypovirus polyhedra</atitle><jtitle>Molecular biology reports</jtitle><stitle>Mol Biol Rep</stitle><addtitle>Mol Biol Rep</addtitle><date>2014</date><risdate>2014</risdate><volume>41</volume><issue>4</issue><spage>2657</spage><epage>2666</epage><pages>2657-2666</pages><issn>0301-4851</issn><eissn>1573-4978</eissn><abstract>To explore whether the nonvirus encoded protein could be embedded into Bombyx mori cypovirus (BmCPV) polyhedra. The stable transformants of BmN cells expressing a polyhedrin (Polh) gene of BmCPV were constructed by transfection with a non-transposon derived vector containing a polh gene. The polyhedra were purified from the midguts of BmCPV-infected silkworms and the transformed BmN cells, respectively. The proteins embedded into polyhedra were determined by mass spectrometry analysis. Host derived proteins were detected in the purified polyhedra. Analysis of structure and hydrophilicity of embedded proteins indicated that the hydrophilic proteins, in structure, were similar to the left-handed structure of polyhedrin or the N-terminal domain of BmCPV structural protein VP3, which were easily embedded into the BmCPV polyhedra. The lysate of polyhedra purified from the infected transformation of BmN cells with modified B. mori baculovirus BmPAK6 could infect BmN cells, indicating that B. mori baculovirus could be embedded into BmCPV polyhedra. Both the purified polyhedra and its lysate could be coloured by X-gal, indicating that the β-galactosidase expressed by BmPAK6 could be incorporated into BmCPV polyhedra. These results suggested that some heterologous proteins and baculovirus could be embedded into polyhedra in an unknown manner.</abstract><cop>Dordrecht</cop><pub>Springer-Verlag</pub><pmid>24469718</pmid><doi>10.1007/s11033-014-3124-7</doi><tpages>10</tpages></addata></record> |
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subjects | Animal Anatomy Animal Biochemistry Animals Baculoviridae Baculoviridae - genetics Baculoviridae - metabolism beta-galactosidase beta-Galactosidase - genetics beta-Galactosidase - metabolism Biomedical and Life Sciences Bombyx - virology Bombyx mori Cell Line Cypovirus genes Histology Host-Pathogen Interactions hydrophilicity Life Sciences Mass spectrometry Models, Molecular Molecular biology Morphology Protein Conformation Proteins Proteins - chemistry Proteins - genetics Proteins - metabolism Reoviridae - physiology silkworms transfection Viral Structural Proteins - chemistry Viral Structural Proteins - metabolism Virus Assembly Viruses |
title | Nonvirus encoded proteins could be embedded into Bombyx mori cypovirus polyhedra |
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