A viral caspase contributes to modified apoptosis for virus transmission
The Spodoptera frugiperda ascovirus, a DNA virus that attacks lepidopterans, codes for an executioner caspase synthesized by 9 h after infection of Sf21 cells. This caspase alone induces apoptosis in insect cells and, during viral replication in vivo, contributes to a novel cell cleavage process in...
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Veröffentlicht in: | Genes & development 2005-06, Vol.19 (12), p.1416-1421 |
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creator | Bideshi, Dennis K Tan, Yeping Bigot, Yves Federici, Brian A |
description | The Spodoptera frugiperda ascovirus, a DNA virus that attacks lepidopterans, codes for an executioner caspase synthesized by 9 h after infection of Sf21 cells. This caspase alone induces apoptosis in insect cells and, during viral replication in vivo, contributes to a novel cell cleavage process in which developing apoptotic bodies are rescued by the virus and differentiate to form large vesicles in which virions assemble. These viral vesicles disseminate to the blood, where they are acquired during egg-laying by parasitic wasps that transmit the virus. No other viruses encode caspases or form such modified apoptotic bodies, suggesting this caspase plays a direct role in cell partitioning that facilitates viral reproduction and transmission. |
doi_str_mv | 10.1101/gad.1300205 |
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This caspase alone induces apoptosis in insect cells and, during viral replication in vivo, contributes to a novel cell cleavage process in which developing apoptotic bodies are rescued by the virus and differentiate to form large vesicles in which virions assemble. These viral vesicles disseminate to the blood, where they are acquired during egg-laying by parasitic wasps that transmit the virus. No other viruses encode caspases or form such modified apoptotic bodies, suggesting this caspase plays a direct role in cell partitioning that facilitates viral reproduction and transmission.</description><identifier>ISSN: 0890-9369</identifier><identifier>EISSN: 1549-5477</identifier><identifier>DOI: 10.1101/gad.1300205</identifier><identifier>PMID: 15933068</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>Amino Acid Sequence ; Animals ; Apoptosis - physiology ; Ascoviridae - enzymology ; Ascoviridae - genetics ; Ascoviridae - pathogenicity ; Caspase 3 ; Caspase 7 ; Caspases - genetics ; Caspases - physiology ; Female ; Humans ; Molecular Sequence Data ; Research Communications ; Sequence Homology, Amino Acid ; Spodoptera - cytology ; Spodoptera - virology ; Virulence - physiology ; Virus Diseases - pathology ; Virus Diseases - transmission</subject><ispartof>Genes & development, 2005-06, Vol.19 (12), p.1416-1421</ispartof><rights>Copyright © 2005, Cold Spring Harbor Laboratory Press 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c410t-6dc80efb30a3918b7ac31a13829c662677aa3d0dd270339ab196f20b570ac8f73</citedby><cites>FETCH-LOGICAL-c410t-6dc80efb30a3918b7ac31a13829c662677aa3d0dd270339ab196f20b570ac8f73</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/PMC1151656/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1151656/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,27911,27912,53778,53780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15933068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bideshi, Dennis K</creatorcontrib><creatorcontrib>Tan, Yeping</creatorcontrib><creatorcontrib>Bigot, Yves</creatorcontrib><creatorcontrib>Federici, Brian A</creatorcontrib><title>A viral caspase contributes to modified apoptosis for virus transmission</title><title>Genes & development</title><addtitle>Genes Dev</addtitle><description>The Spodoptera frugiperda ascovirus, a DNA virus that attacks lepidopterans, codes for an executioner caspase synthesized by 9 h after infection of Sf21 cells. This caspase alone induces apoptosis in insect cells and, during viral replication in vivo, contributes to a novel cell cleavage process in which developing apoptotic bodies are rescued by the virus and differentiate to form large vesicles in which virions assemble. These viral vesicles disseminate to the blood, where they are acquired during egg-laying by parasitic wasps that transmit the virus. No other viruses encode caspases or form such modified apoptotic bodies, suggesting this caspase plays a direct role in cell partitioning that facilitates viral reproduction and transmission.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Apoptosis - physiology</subject><subject>Ascoviridae - enzymology</subject><subject>Ascoviridae - genetics</subject><subject>Ascoviridae - pathogenicity</subject><subject>Caspase 3</subject><subject>Caspase 7</subject><subject>Caspases - genetics</subject><subject>Caspases - physiology</subject><subject>Female</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Research Communications</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spodoptera - cytology</subject><subject>Spodoptera - virology</subject><subject>Virulence - physiology</subject><subject>Virus Diseases - pathology</subject><subject>Virus Diseases - transmission</subject><issn>0890-9369</issn><issn>1549-5477</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1LxDAQxYMouq6evEtPXqTrTNMmzUUQUVdY8KLnME1TjXSbmrSC_71dXPw4eZrD-83jPR5jJwgLRMCLZ6oXyAEyKHbYDItcpUUu5S6bQakgVVyoA3YY4ysACBBinx1goTgHUc7Y8ip5d4HaxFDsKdrE-G4IrhoHG5PBJ2tfu8bZOqHe94OPLiaND5ufcdIDdXHtYnS-O2J7DbXRHm_vnD3d3jxeL9PVw9399dUqNTnCkIralGCbigNxhWUlyXAk5GWmjBCZkJKI11DXmQTOFVWoRJNBVUggUzaSz9nll28_VmtbGzvFpVb3wa0pfGhPTv9VOvein_27RixQFGIyONsaBP822jjoqYGxbUud9WPUQqqcF5n8F0QpchAcJvD8CzTBxxhs850GQW8m0tNEejvRRJ_-LvDDbjfhn1_Rjbg</recordid><startdate>20050615</startdate><enddate>20050615</enddate><creator>Bideshi, Dennis K</creator><creator>Tan, Yeping</creator><creator>Bigot, Yves</creator><creator>Federici, Brian A</creator><general>Cold Spring Harbor Laboratory Press</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>7SS</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050615</creationdate><title>A viral caspase contributes to modified apoptosis for virus transmission</title><author>Bideshi, Dennis K ; 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subjects | Amino Acid Sequence Animals Apoptosis - physiology Ascoviridae - enzymology Ascoviridae - genetics Ascoviridae - pathogenicity Caspase 3 Caspase 7 Caspases - genetics Caspases - physiology Female Humans Molecular Sequence Data Research Communications Sequence Homology, Amino Acid Spodoptera - cytology Spodoptera - virology Virulence - physiology Virus Diseases - pathology Virus Diseases - transmission |
title | A viral caspase contributes to modified apoptosis for virus transmission |
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