Presentation of functional foreign peptides on the surface of SV40 virus-like particles
Viral capsids of simian virus 40 (SV40) are highly efficient gene delivery vehicles that infect a broad range of cells and tissues. To develop a controlled, cell type-specific delivery system, we sought to display foreign peptides on the capsid surface by genetically manipulating the major capsid pr...
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| Veröffentlicht in: | Journal of biotechnology 2008-07, Vol.135 (4), p.385-392 |
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| creator | Takahashi, Ryou-u Kanesashi, Shin-nosuke Inoue, Takamasa Enomoto, Teruya Kawano, Masa-aki Tsukamoto, Hiroko Takeshita, Fumitaka Imai, Takeshi Ochiya, Takahiro Kataoka, Kohsuke Yamaguchi, Yuki Handa, Hiroshi |
| description | Viral capsids of simian virus 40 (SV40) are highly efficient gene delivery vehicles that infect a broad range of cells and tissues. To develop a controlled, cell type-specific delivery system, we sought to display foreign peptides on the capsid surface by genetically manipulating the major capsid protein Vp1. Here we report the identification of two sites within the surface loops of Vp1 that can accommodate foreign peptides in such a way that the foreign peptides are displayed on the surface of the virus-like particles (VLPs) without interfering with VLP assembly or the packaging of viral DNA. Insertion of Flag-tags but not RGD integrin-binding motifs at these sites strongly inhibited cell attachment of VLPs, which normally associate with host cells through cell surface molecules such as major histocompatibility complex (MHC) class I and ganglioside GM1. Instead, VLPs carrying the RGD motifs bound to integrin
in vitro and to the cell surface in an RGD-dependent manner. Thus, insertion of foreign sequences into the surface loops of Vp1 can reduce natural virus–cell interactions and even confer an ability to bind to a new target receptor. This study demonstrates the potential usefulness of this strategy for the development of novel delivery vehicles with different cell tropisms. |
| doi_str_mv | 10.1016/j.jbiotec.2008.05.012 |
| format | Article |
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in vitro and to the cell surface in an RGD-dependent manner. Thus, insertion of foreign sequences into the surface loops of Vp1 can reduce natural virus–cell interactions and even confer an ability to bind to a new target receptor. This study demonstrates the potential usefulness of this strategy for the development of novel delivery vehicles with different cell tropisms.</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/j.jbiotec.2008.05.012</identifier><identifier>PMID: 18588926</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Biological and medical sciences ; Biotechnology ; Capsid ; Capsid Proteins - metabolism ; Cell Adhesion ; Cercopithecus aethiops ; COS Cells ; DNA Packaging ; DNA, Viral - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycine ; Integrin ; Integrin alphaVbeta3 - metabolism ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutant Proteins - metabolism ; Oligopeptides ; Peptides - metabolism ; Protein Structure, Secondary ; Recombinant Fusion Proteins - metabolism ; RGD ; Simian virus 40 ; Simian virus 40 - metabolism ; SV40 ; Tropism ; Viral Fusion Proteins - chemistry ; Viral Fusion Proteins - metabolism ; Virion - metabolism ; VLP</subject><ispartof>Journal of biotechnology, 2008-07, Vol.135 (4), p.385-392</ispartof><rights>2008 Elsevier B.V.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c558t-b029092ffd902aeec0d4395e0c4804e38bdaa13c0c1c5dadd1f7300ddfd8b59f3</citedby><cites>FETCH-LOGICAL-c558t-b029092ffd902aeec0d4395e0c4804e38bdaa13c0c1c5dadd1f7300ddfd8b59f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0168165608002344$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20561515$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18588926$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takahashi, Ryou-u</creatorcontrib><creatorcontrib>Kanesashi, Shin-nosuke</creatorcontrib><creatorcontrib>Inoue, Takamasa</creatorcontrib><creatorcontrib>Enomoto, Teruya</creatorcontrib><creatorcontrib>Kawano, Masa-aki</creatorcontrib><creatorcontrib>Tsukamoto, Hiroko</creatorcontrib><creatorcontrib>Takeshita, Fumitaka</creatorcontrib><creatorcontrib>Imai, Takeshi</creatorcontrib><creatorcontrib>Ochiya, Takahiro</creatorcontrib><creatorcontrib>Kataoka, Kohsuke</creatorcontrib><creatorcontrib>Yamaguchi, Yuki</creatorcontrib><creatorcontrib>Handa, Hiroshi</creatorcontrib><title>Presentation of functional foreign peptides on the surface of SV40 virus-like particles</title><title>Journal of biotechnology</title><addtitle>J Biotechnol</addtitle><description>Viral capsids of simian virus 40 (SV40) are highly efficient gene delivery vehicles that infect a broad range of cells and tissues. To develop a controlled, cell type-specific delivery system, we sought to display foreign peptides on the capsid surface by genetically manipulating the major capsid protein Vp1. Here we report the identification of two sites within the surface loops of Vp1 that can accommodate foreign peptides in such a way that the foreign peptides are displayed on the surface of the virus-like particles (VLPs) without interfering with VLP assembly or the packaging of viral DNA. Insertion of Flag-tags but not RGD integrin-binding motifs at these sites strongly inhibited cell attachment of VLPs, which normally associate with host cells through cell surface molecules such as major histocompatibility complex (MHC) class I and ganglioside GM1. Instead, VLPs carrying the RGD motifs bound to integrin
in vitro and to the cell surface in an RGD-dependent manner. Thus, insertion of foreign sequences into the surface loops of Vp1 can reduce natural virus–cell interactions and even confer an ability to bind to a new target receptor. This study demonstrates the potential usefulness of this strategy for the development of novel delivery vehicles with different cell tropisms.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Capsid</subject><subject>Capsid Proteins - metabolism</subject><subject>Cell Adhesion</subject><subject>Cercopithecus aethiops</subject><subject>COS Cells</subject><subject>DNA Packaging</subject><subject>DNA, Viral - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycine</subject><subject>Integrin</subject><subject>Integrin alphaVbeta3 - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Insertional</subject><subject>Mutant Proteins - metabolism</subject><subject>Oligopeptides</subject><subject>Peptides - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RGD</subject><subject>Simian virus 40</subject><subject>Simian virus 40 - metabolism</subject><subject>SV40</subject><subject>Tropism</subject><subject>Viral Fusion Proteins - chemistry</subject><subject>Viral Fusion Proteins - metabolism</subject><subject>Virion - metabolism</subject><subject>VLP</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0Mtu1DAUgGELgei09BGAbOgu4diJM_YKoYqbVKmVSunScuzj4iETp7ZTibfHo4lgycpefMeXn5DXFBoKtH-_a3aDDxlNwwBEA7wByp6RDRXbtu5E3z4nm-JETXven5DTlHYA0ElOX5ITKrgQkvUbcn8TMeGUdfZhqoKr3DKZw16PlQsR_cNUzThnbzFVReSfWKUlOm3woG9_dFA9-bikevS_sJp1zN6MmF6RF06PCc_X9Yzcff70_fJrfXX95dvlx6vacC5yPQCTIJlzVgLTiAZs10qOYDoBHbZisFrT1oChhlttLXXbFsBaZ8XApWvPyMXx3DmGxwVTVnufDI6jnjAsSTGQLRewLZAfoYkhpYhOzdHvdfytKKhDUbVTa1F1KKqAq1K0zL1ZL1iGPdp_U2vCAt6tQCejRxf1ZHz66xjwnnLKi3t7dE4HpR9iMXe3DGj5jqRbDm0RH44CS7Anj1El43EyaH1Ek5UN_j-P_QNe8aFC</recordid><startdate>20080731</startdate><enddate>20080731</enddate><creator>Takahashi, Ryou-u</creator><creator>Kanesashi, Shin-nosuke</creator><creator>Inoue, Takamasa</creator><creator>Enomoto, Teruya</creator><creator>Kawano, Masa-aki</creator><creator>Tsukamoto, Hiroko</creator><creator>Takeshita, Fumitaka</creator><creator>Imai, Takeshi</creator><creator>Ochiya, Takahiro</creator><creator>Kataoka, Kohsuke</creator><creator>Yamaguchi, Yuki</creator><creator>Handa, Hiroshi</creator><general>Elsevier B.V</general><general>[New York, NY]: Elsevier</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</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>7QO</scope><scope>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope></search><sort><creationdate>20080731</creationdate><title>Presentation of functional foreign peptides on the surface of SV40 virus-like particles</title><author>Takahashi, Ryou-u ; Kanesashi, Shin-nosuke ; Inoue, Takamasa ; Enomoto, Teruya ; Kawano, Masa-aki ; Tsukamoto, Hiroko ; Takeshita, Fumitaka ; Imai, Takeshi ; Ochiya, Takahiro ; Kataoka, Kohsuke ; Yamaguchi, Yuki ; Handa, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-b029092ffd902aeec0d4395e0c4804e38bdaa13c0c1c5dadd1f7300ddfd8b59f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Capsid</topic><topic>Capsid Proteins - metabolism</topic><topic>Cell Adhesion</topic><topic>Cercopithecus aethiops</topic><topic>COS Cells</topic><topic>DNA Packaging</topic><topic>DNA, Viral - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycine</topic><topic>Integrin</topic><topic>Integrin alphaVbeta3 - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Insertional</topic><topic>Mutant Proteins - metabolism</topic><topic>Oligopeptides</topic><topic>Peptides - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>RGD</topic><topic>Simian virus 40</topic><topic>Simian virus 40 - metabolism</topic><topic>SV40</topic><topic>Tropism</topic><topic>Viral Fusion Proteins - chemistry</topic><topic>Viral Fusion Proteins - metabolism</topic><topic>Virion - metabolism</topic><topic>VLP</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takahashi, Ryou-u</creatorcontrib><creatorcontrib>Kanesashi, Shin-nosuke</creatorcontrib><creatorcontrib>Inoue, Takamasa</creatorcontrib><creatorcontrib>Enomoto, Teruya</creatorcontrib><creatorcontrib>Kawano, Masa-aki</creatorcontrib><creatorcontrib>Tsukamoto, Hiroko</creatorcontrib><creatorcontrib>Takeshita, Fumitaka</creatorcontrib><creatorcontrib>Imai, Takeshi</creatorcontrib><creatorcontrib>Ochiya, Takahiro</creatorcontrib><creatorcontrib>Kataoka, Kohsuke</creatorcontrib><creatorcontrib>Yamaguchi, Yuki</creatorcontrib><creatorcontrib>Handa, Hiroshi</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takahashi, Ryou-u</au><au>Kanesashi, Shin-nosuke</au><au>Inoue, Takamasa</au><au>Enomoto, Teruya</au><au>Kawano, Masa-aki</au><au>Tsukamoto, Hiroko</au><au>Takeshita, Fumitaka</au><au>Imai, Takeshi</au><au>Ochiya, Takahiro</au><au>Kataoka, Kohsuke</au><au>Yamaguchi, Yuki</au><au>Handa, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Presentation of functional foreign peptides on the surface of SV40 virus-like particles</atitle><jtitle>Journal of biotechnology</jtitle><addtitle>J Biotechnol</addtitle><date>2008-07-31</date><risdate>2008</risdate><volume>135</volume><issue>4</issue><spage>385</spage><epage>392</epage><pages>385-392</pages><issn>0168-1656</issn><eissn>1873-4863</eissn><coden>JBITD4</coden><abstract>Viral capsids of simian virus 40 (SV40) are highly efficient gene delivery vehicles that infect a broad range of cells and tissues. To develop a controlled, cell type-specific delivery system, we sought to display foreign peptides on the capsid surface by genetically manipulating the major capsid protein Vp1. Here we report the identification of two sites within the surface loops of Vp1 that can accommodate foreign peptides in such a way that the foreign peptides are displayed on the surface of the virus-like particles (VLPs) without interfering with VLP assembly or the packaging of viral DNA. Insertion of Flag-tags but not RGD integrin-binding motifs at these sites strongly inhibited cell attachment of VLPs, which normally associate with host cells through cell surface molecules such as major histocompatibility complex (MHC) class I and ganglioside GM1. Instead, VLPs carrying the RGD motifs bound to integrin
in vitro and to the cell surface in an RGD-dependent manner. Thus, insertion of foreign sequences into the surface loops of Vp1 can reduce natural virus–cell interactions and even confer an ability to bind to a new target receptor. This study demonstrates the potential usefulness of this strategy for the development of novel delivery vehicles with different cell tropisms.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>18588926</pmid><doi>10.1016/j.jbiotec.2008.05.012</doi><tpages>8</tpages></addata></record> |
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| ispartof | Journal of biotechnology, 2008-07, Vol.135 (4), p.385-392 |
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| subjects | Amino Acid Motifs Amino Acid Sequence Animals Biological and medical sciences Biotechnology Capsid Capsid Proteins - metabolism Cell Adhesion Cercopithecus aethiops COS Cells DNA Packaging DNA, Viral - metabolism Fundamental and applied biological sciences. Psychology Glycine Integrin Integrin alphaVbeta3 - metabolism Molecular Sequence Data Mutagenesis, Insertional Mutant Proteins - metabolism Oligopeptides Peptides - metabolism Protein Structure, Secondary Recombinant Fusion Proteins - metabolism RGD Simian virus 40 Simian virus 40 - metabolism SV40 Tropism Viral Fusion Proteins - chemistry Viral Fusion Proteins - metabolism Virion - metabolism VLP |
| title | Presentation of functional foreign peptides on the surface of SV40 virus-like particles |
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