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Inhibition of TNF receptor 1 internalization by adenovirus 14.7K as a novel immune escape mechanism
The adenoviral protein E3-14.7K (14.7K) is an inhibitor of TNF-induced apoptosis, but the molecular mechanism underlying this protective effect has not yet been explained exhaustively. TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD),...
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Published in: | The Journal of clinical investigation 2006-11, Vol.116 (11), p.2901-2913 |
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creator | Schneider-Brachert, Wulf Tchikov, Vladimir Merkel, Oliver Jakob, Marten Hallas, Cora Kruse, Marie-Luise Groitl, Peter Lehn, Alexander Hildt, Eberhard Held-Feindt, Janka Dobner, Thomas Kabelitz, Dieter Krönke, Martin Schütze, Stefan |
description | The adenoviral protein E3-14.7K (14.7K) is an inhibitor of TNF-induced apoptosis, but the molecular mechanism underlying this protective effect has not yet been explained exhaustively. TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD), Fas-associated death domain (FADD), and caspase-8 to the death domain of TNF receptor 1 (TNFR1), thereby establishing the death-inducing signaling complex (DISC). Here we report that adenovirus 14.7K protein inhibits ligand-induced TNFR1 internalization. Analysis of purified magnetically labeled TNFR1 complexes from murine and human cells stably transduced with 14.7K revealed that prevention of TNFR1 internalization resulted in inhibition of DISC formation. In contrast, 14.7K did not affect TNF-induced NF-kappaB activation via recruitment of receptor-interacting protein 1 (RIP-1) and TNF receptor-associated factor 2 (TRAF-2). Inhibition of endocytosis by 14.7K was effected by failure of coordinated temporal and spatial assembly of essential components of the endocytic machinery such as Rab5 and dynamin 2 at the site of the activated TNFR1. Furthermore, we found that the same TNF defense mechanisms were instrumental in protecting wild-type adenovirus-infected human cells expressing 14.7K. This study describes a new molecular mechanism implemented by a virus to escape immunosurveillance by selectively targeting TNFR1 endocytosis to prevent TNF-induced DISC formation. |
doi_str_mv | 10.1172/jci23771 |
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TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD), Fas-associated death domain (FADD), and caspase-8 to the death domain of TNF receptor 1 (TNFR1), thereby establishing the death-inducing signaling complex (DISC). Here we report that adenovirus 14.7K protein inhibits ligand-induced TNFR1 internalization. Analysis of purified magnetically labeled TNFR1 complexes from murine and human cells stably transduced with 14.7K revealed that prevention of TNFR1 internalization resulted in inhibition of DISC formation. In contrast, 14.7K did not affect TNF-induced NF-kappaB activation via recruitment of receptor-interacting protein 1 (RIP-1) and TNF receptor-associated factor 2 (TRAF-2). Inhibition of endocytosis by 14.7K was effected by failure of coordinated temporal and spatial assembly of essential components of the endocytic machinery such as Rab5 and dynamin 2 at the site of the activated TNFR1. Furthermore, we found that the same TNF defense mechanisms were instrumental in protecting wild-type adenovirus-infected human cells expressing 14.7K. This study describes a new molecular mechanism implemented by a virus to escape immunosurveillance by selectively targeting TNFR1 endocytosis to prevent TNF-induced DISC formation.</description><identifier>ISSN: 0021-9738</identifier><identifier>EISSN: 1558-8238</identifier><identifier>DOI: 10.1172/jci23771</identifier><identifier>PMID: 17024246</identifier><language>eng</language><publisher>United States: American Society for Clinical Investigation</publisher><subject>Adenoviridae - immunology ; Adenovirus E3 Proteins - genetics ; Adenovirus E3 Proteins - immunology ; Adenovirus E3 Proteins - metabolism ; Adenoviruses ; Analysis ; Animals ; Apoptosis ; Biomedical research ; Cell Line ; Cells ; Cytotoxicity ; Death Domain Receptor Signaling Adaptor Proteins - metabolism ; Defense mechanisms ; Endocytosis ; Humans ; Ligands ; Mice ; NF-kappa B - metabolism ; Proteins ; Receptors, Tumor Necrosis Factor - antagonists & inhibitors ; Receptors, Tumor Necrosis Factor - immunology ; Receptors, Tumor Necrosis Factor - metabolism ; Recruitment ; Tumor necrosis factor ; Tumor Necrosis Factor-alpha - metabolism ; Virus Internalization</subject><ispartof>The Journal of clinical investigation, 2006-11, Vol.116 (11), p.2901-2913</ispartof><rights>COPYRIGHT 2006 American Society for Clinical Investigation</rights><rights>Copyright American Society for Clinical Investigation Nov 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c562t-cb60b7dfa6366742c459b8cb686e8b4b7c339ab7fe572d8c32efb6dad3bc3dad3</citedby><cites>FETCH-LOGICAL-c562t-cb60b7dfa6366742c459b8cb686e8b4b7c339ab7fe572d8c32efb6dad3bc3dad3</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/PMC1590267/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1590267/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17024246$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schneider-Brachert, Wulf</creatorcontrib><creatorcontrib>Tchikov, Vladimir</creatorcontrib><creatorcontrib>Merkel, Oliver</creatorcontrib><creatorcontrib>Jakob, Marten</creatorcontrib><creatorcontrib>Hallas, Cora</creatorcontrib><creatorcontrib>Kruse, Marie-Luise</creatorcontrib><creatorcontrib>Groitl, Peter</creatorcontrib><creatorcontrib>Lehn, Alexander</creatorcontrib><creatorcontrib>Hildt, Eberhard</creatorcontrib><creatorcontrib>Held-Feindt, Janka</creatorcontrib><creatorcontrib>Dobner, Thomas</creatorcontrib><creatorcontrib>Kabelitz, Dieter</creatorcontrib><creatorcontrib>Krönke, Martin</creatorcontrib><creatorcontrib>Schütze, Stefan</creatorcontrib><title>Inhibition of TNF receptor 1 internalization by adenovirus 14.7K as a novel immune escape mechanism</title><title>The Journal of clinical investigation</title><addtitle>J Clin Invest</addtitle><description>The adenoviral protein E3-14.7K (14.7K) is an inhibitor of TNF-induced apoptosis, but the molecular mechanism underlying this protective effect has not yet been explained exhaustively. TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD), Fas-associated death domain (FADD), and caspase-8 to the death domain of TNF receptor 1 (TNFR1), thereby establishing the death-inducing signaling complex (DISC). Here we report that adenovirus 14.7K protein inhibits ligand-induced TNFR1 internalization. Analysis of purified magnetically labeled TNFR1 complexes from murine and human cells stably transduced with 14.7K revealed that prevention of TNFR1 internalization resulted in inhibition of DISC formation. In contrast, 14.7K did not affect TNF-induced NF-kappaB activation via recruitment of receptor-interacting protein 1 (RIP-1) and TNF receptor-associated factor 2 (TRAF-2). Inhibition of endocytosis by 14.7K was effected by failure of coordinated temporal and spatial assembly of essential components of the endocytic machinery such as Rab5 and dynamin 2 at the site of the activated TNFR1. Furthermore, we found that the same TNF defense mechanisms were instrumental in protecting wild-type adenovirus-infected human cells expressing 14.7K. This study describes a new molecular mechanism implemented by a virus to escape immunosurveillance by selectively targeting TNFR1 endocytosis to prevent TNF-induced DISC formation.</description><subject>Adenoviridae - immunology</subject><subject>Adenovirus E3 Proteins - genetics</subject><subject>Adenovirus E3 Proteins - immunology</subject><subject>Adenovirus E3 Proteins - metabolism</subject><subject>Adenoviruses</subject><subject>Analysis</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biomedical research</subject><subject>Cell Line</subject><subject>Cells</subject><subject>Cytotoxicity</subject><subject>Death Domain Receptor Signaling Adaptor Proteins - metabolism</subject><subject>Defense mechanisms</subject><subject>Endocytosis</subject><subject>Humans</subject><subject>Ligands</subject><subject>Mice</subject><subject>NF-kappa B - metabolism</subject><subject>Proteins</subject><subject>Receptors, Tumor Necrosis Factor - antagonists & inhibitors</subject><subject>Receptors, Tumor Necrosis Factor - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of clinical investigation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schneider-Brachert, Wulf</au><au>Tchikov, Vladimir</au><au>Merkel, Oliver</au><au>Jakob, Marten</au><au>Hallas, Cora</au><au>Kruse, Marie-Luise</au><au>Groitl, Peter</au><au>Lehn, Alexander</au><au>Hildt, Eberhard</au><au>Held-Feindt, Janka</au><au>Dobner, Thomas</au><au>Kabelitz, Dieter</au><au>Krönke, Martin</au><au>Schütze, Stefan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition of TNF receptor 1 internalization by adenovirus 14.7K as a novel immune escape mechanism</atitle><jtitle>The Journal of clinical investigation</jtitle><addtitle>J Clin Invest</addtitle><date>2006-11-01</date><risdate>2006</risdate><volume>116</volume><issue>11</issue><spage>2901</spage><epage>2913</epage><pages>2901-2913</pages><issn>0021-9738</issn><eissn>1558-8238</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The adenoviral protein E3-14.7K (14.7K) is an inhibitor of TNF-induced apoptosis, but the molecular mechanism underlying this protective effect has not yet been explained exhaustively. TNF-mediated apoptosis is initiated by ligand-induced recruitment of TNF receptor-associated death domain (TRADD), Fas-associated death domain (FADD), and caspase-8 to the death domain of TNF receptor 1 (TNFR1), thereby establishing the death-inducing signaling complex (DISC). Here we report that adenovirus 14.7K protein inhibits ligand-induced TNFR1 internalization. Analysis of purified magnetically labeled TNFR1 complexes from murine and human cells stably transduced with 14.7K revealed that prevention of TNFR1 internalization resulted in inhibition of DISC formation. In contrast, 14.7K did not affect TNF-induced NF-kappaB activation via recruitment of receptor-interacting protein 1 (RIP-1) and TNF receptor-associated factor 2 (TRAF-2). Inhibition of endocytosis by 14.7K was effected by failure of coordinated temporal and spatial assembly of essential components of the endocytic machinery such as Rab5 and dynamin 2 at the site of the activated TNFR1. Furthermore, we found that the same TNF defense mechanisms were instrumental in protecting wild-type adenovirus-infected human cells expressing 14.7K. This study describes a new molecular mechanism implemented by a virus to escape immunosurveillance by selectively targeting TNFR1 endocytosis to prevent TNF-induced DISC formation.</abstract><cop>United States</cop><pub>American Society for Clinical Investigation</pub><pmid>17024246</pmid><doi>10.1172/jci23771</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adenoviridae - immunology Adenovirus E3 Proteins - genetics Adenovirus E3 Proteins - immunology Adenovirus E3 Proteins - metabolism Adenoviruses Analysis Animals Apoptosis Biomedical research Cell Line Cells Cytotoxicity Death Domain Receptor Signaling Adaptor Proteins - metabolism Defense mechanisms Endocytosis Humans Ligands Mice NF-kappa B - metabolism Proteins Receptors, Tumor Necrosis Factor - antagonists & inhibitors Receptors, Tumor Necrosis Factor - immunology Receptors, Tumor Necrosis Factor - metabolism Recruitment Tumor necrosis factor Tumor Necrosis Factor-alpha - metabolism Virus Internalization |
title | Inhibition of TNF receptor 1 internalization by adenovirus 14.7K as a novel immune escape mechanism |
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