Processing of Human Toll-like Receptor 7 by Furin-like Proprotein Convertases Is Required for Its Accumulation and Activity in Endosomes
Toll-like receptor 7 (TLR7) triggers antiviral immune responses by recognizing viral single-stranded RNA in endosomes, but the biosynthetic pathway of human TLR7 (hTLR7) remains unclear. Here, we show that hTLR7 is proteolytically processed and that the C-terminal fragment selectively accumulates in...
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| Veröffentlicht in: | Immunity (Cambridge, Mass.) Mass.), 2013-10, Vol.39 (4), p.711-721 |
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| creator | Hipp, Madeleine M. Shepherd, Dawn Gileadi, Uzi Aichinger, Michael C. Kessler, Benedikt M. Edelmann, Mariola J. Essalmani, Rachid Seidah, Nabil G. Reis e Sousa, Caetano Cerundolo, Vincenzo |
| description | Toll-like receptor 7 (TLR7) triggers antiviral immune responses by recognizing viral single-stranded RNA in endosomes, but the biosynthetic pathway of human TLR7 (hTLR7) remains unclear. Here, we show that hTLR7 is proteolytically processed and that the C-terminal fragment selectively accumulates in endocytic compartments. hTLR7 processing occurred at neutral pH and was dependent on furin-like proprotein convertases (PCs). Furthermore, TLR7 processing was required for its functional response to TLR7 agonists such as R837 or influenza virus. Notably, proinflammatory and differentiation stimuli increased the expression of furin-like PCs in immune cells, suggesting a positive feedback mechanism for TLR7 processing during infection. Because self-RNA can under certain conditions activate TLR7 and trigger autoimmunity, our results identify furin-like PCs as a possible target to attenuate TLR7-dependent autoimmunity and other immune pathologies.
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•Human TLR7 is cleaved and accumulates in endosomes independently of low pH•Calcium-dependent furin-like proprotein convertases (PCs) process TLR7•Inhibition or knockdown of furin-like PCs reduces responsiveness to TLR7 agonists•Mutating a furin-like PC recognition site in TLR7 reduces receptor processing |
| doi_str_mv | 10.1016/j.immuni.2013.09.004 |
| format | Article |
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[Display omitted]
•Human TLR7 is cleaved and accumulates in endosomes independently of low pH•Calcium-dependent furin-like proprotein convertases (PCs) process TLR7•Inhibition or knockdown of furin-like PCs reduces responsiveness to TLR7 agonists•Mutating a furin-like PC recognition site in TLR7 reduces receptor processing</description><identifier>ISSN: 1074-7613</identifier><identifier>EISSN: 1097-4180</identifier><identifier>DOI: 10.1016/j.immuni.2013.09.004</identifier><identifier>PMID: 24138882</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Autoimmunity ; Biomedical research ; Cell Line ; Endosomes - drug effects ; Endosomes - immunology ; Enzymes ; Feedback, Physiological ; Furin - genetics ; Furin - immunology ; Furin - metabolism ; Gene Expression Regulation ; Genetic Vectors ; Humans ; Influenza virus ; Lentivirus - genetics ; Ligands ; Macrophages - cytology ; Macrophages - drug effects ; Macrophages - immunology ; Macrophages - metabolism ; Mass spectrometry ; Medical research ; Molecular Sequence Data ; Orthomyxoviridae - immunology ; Polypeptides ; Proprotein Convertases - genetics ; Proprotein Convertases - immunology ; Proprotein Convertases - metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Quinolines - pharmacology ; Signal Transduction ; Toll-Like Receptor 7 - genetics ; Toll-Like Receptor 7 - immunology ; Toll-Like Receptor 7 - metabolism</subject><ispartof>Immunity (Cambridge, Mass.), 2013-10, Vol.39 (4), p.711-721</ispartof><rights>2013 Elsevier Inc.</rights><rights>Copyright © 2013 Elsevier Inc. All rights reserved.</rights><rights>Copyright Elsevier Limited Oct 17, 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c590t-9db37e230e7a0cfd2d809448355c051fbb2c6210a11c03ca198edcafeb7f5043</citedby><cites>FETCH-LOGICAL-c590t-9db37e230e7a0cfd2d809448355c051fbb2c6210a11c03ca198edcafeb7f5043</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1074761313004263$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24138882$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hipp, Madeleine M.</creatorcontrib><creatorcontrib>Shepherd, Dawn</creatorcontrib><creatorcontrib>Gileadi, Uzi</creatorcontrib><creatorcontrib>Aichinger, Michael C.</creatorcontrib><creatorcontrib>Kessler, Benedikt M.</creatorcontrib><creatorcontrib>Edelmann, Mariola J.</creatorcontrib><creatorcontrib>Essalmani, Rachid</creatorcontrib><creatorcontrib>Seidah, Nabil G.</creatorcontrib><creatorcontrib>Reis e Sousa, Caetano</creatorcontrib><creatorcontrib>Cerundolo, Vincenzo</creatorcontrib><title>Processing of Human Toll-like Receptor 7 by Furin-like Proprotein Convertases Is Required for Its Accumulation and Activity in Endosomes</title><title>Immunity (Cambridge, Mass.)</title><addtitle>Immunity</addtitle><description>Toll-like receptor 7 (TLR7) triggers antiviral immune responses by recognizing viral single-stranded RNA in endosomes, but the biosynthetic pathway of human TLR7 (hTLR7) remains unclear. Here, we show that hTLR7 is proteolytically processed and that the C-terminal fragment selectively accumulates in endocytic compartments. hTLR7 processing occurred at neutral pH and was dependent on furin-like proprotein convertases (PCs). Furthermore, TLR7 processing was required for its functional response to TLR7 agonists such as R837 or influenza virus. Notably, proinflammatory and differentiation stimuli increased the expression of furin-like PCs in immune cells, suggesting a positive feedback mechanism for TLR7 processing during infection. Because self-RNA can under certain conditions activate TLR7 and trigger autoimmunity, our results identify furin-like PCs as a possible target to attenuate TLR7-dependent autoimmunity and other immune pathologies.
[Display omitted]
•Human TLR7 is cleaved and accumulates in endosomes independently of low pH•Calcium-dependent furin-like proprotein convertases (PCs) process TLR7•Inhibition or knockdown of furin-like PCs reduces responsiveness to TLR7 agonists•Mutating a furin-like PC recognition site in TLR7 reduces receptor processing</description><subject>Amino Acid Sequence</subject><subject>Autoimmunity</subject><subject>Biomedical research</subject><subject>Cell Line</subject><subject>Endosomes - drug effects</subject><subject>Endosomes - immunology</subject><subject>Enzymes</subject><subject>Feedback, Physiological</subject><subject>Furin - genetics</subject><subject>Furin - immunology</subject><subject>Furin - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Genetic Vectors</subject><subject>Humans</subject><subject>Influenza virus</subject><subject>Lentivirus - genetics</subject><subject>Ligands</subject><subject>Macrophages - cytology</subject><subject>Macrophages - drug effects</subject><subject>Macrophages - immunology</subject><subject>Macrophages - metabolism</subject><subject>Mass spectrometry</subject><subject>Medical research</subject><subject>Molecular Sequence Data</subject><subject>Orthomyxoviridae - immunology</subject><subject>Polypeptides</subject><subject>Proprotein Convertases - genetics</subject><subject>Proprotein Convertases - immunology</subject><subject>Proprotein Convertases - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Tertiary</subject><subject>Quinolines - pharmacology</subject><subject>Signal Transduction</subject><subject>Toll-Like Receptor 7 - genetics</subject><subject>Toll-Like Receptor 7 - immunology</subject><subject>Toll-Like Receptor 7 - metabolism</subject><issn>1074-7613</issn><issn>1097-4180</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUstu1DAUjRCIPuAPELLEhk3CdexM7A1SNWrpSJVAaPaW49wUD4k9tZ2R5g_62XiYtjwWsPKV7znnvk5RvKFQUaCLD5vKTtPsbFUDZRXICoA_K04pyLbkVMDzQ9zysl1QdlKcxbgBoLyR8LI4qTllQoj6tLj_ErzBGK27JX4g1_OkHVn7cSxH-x3JVzS4TT6QlnR7cjUH646JTNsGn9A6svRuhyHpiJGsYqbczTZgT4ZMW6VILoyZp3nUyXpHtOvzR7I7m_Ykky9d76OfML4qXgx6jPj64T0v1leX6-V1efP502p5cVOa3HoqZd-xFmsG2GowQ1_3AiTngjWNgYYOXVebRU1BU2qAGU2lwN7oAbt2aICz8-LjUXY7d1POoEtBj2ob7KTDXnlt1Z8ZZ7-pW79TuYTkcpEF3j8IBH83Y0xqstHgOGqHfo6KNg2XXAgq_g_lnEnZMtFm6Lu_oBs_B5cXcRCEfFS-gIziR5QJPsaAw1PfFNTBFGqjjqZQB1MokAp-zvz295mfSI8u-LUUzIvfWQwqGovOYJ8PaZLqvf13hR_xIsxi</recordid><startdate>20131017</startdate><enddate>20131017</enddate><creator>Hipp, Madeleine M.</creator><creator>Shepherd, Dawn</creator><creator>Gileadi, Uzi</creator><creator>Aichinger, Michael C.</creator><creator>Kessler, Benedikt M.</creator><creator>Edelmann, Mariola J.</creator><creator>Essalmani, Rachid</creator><creator>Seidah, Nabil G.</creator><creator>Reis e Sousa, Caetano</creator><creator>Cerundolo, Vincenzo</creator><general>Elsevier Inc</general><general>Elsevier Limited</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>NAPCQ</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20131017</creationdate><title>Processing of Human Toll-like Receptor 7 by Furin-like Proprotein Convertases Is Required for Its Accumulation and Activity in Endosomes</title><author>Hipp, Madeleine M. ; 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Here, we show that hTLR7 is proteolytically processed and that the C-terminal fragment selectively accumulates in endocytic compartments. hTLR7 processing occurred at neutral pH and was dependent on furin-like proprotein convertases (PCs). Furthermore, TLR7 processing was required for its functional response to TLR7 agonists such as R837 or influenza virus. Notably, proinflammatory and differentiation stimuli increased the expression of furin-like PCs in immune cells, suggesting a positive feedback mechanism for TLR7 processing during infection. Because self-RNA can under certain conditions activate TLR7 and trigger autoimmunity, our results identify furin-like PCs as a possible target to attenuate TLR7-dependent autoimmunity and other immune pathologies.
[Display omitted]
•Human TLR7 is cleaved and accumulates in endosomes independently of low pH•Calcium-dependent furin-like proprotein convertases (PCs) process TLR7•Inhibition or knockdown of furin-like PCs reduces responsiveness to TLR7 agonists•Mutating a furin-like PC recognition site in TLR7 reduces receptor processing</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>24138882</pmid><doi>10.1016/j.immuni.2013.09.004</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Immunity (Cambridge, Mass.), 2013-10, Vol.39 (4), p.711-721 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Sequence Autoimmunity Biomedical research Cell Line Endosomes - drug effects Endosomes - immunology Enzymes Feedback, Physiological Furin - genetics Furin - immunology Furin - metabolism Gene Expression Regulation Genetic Vectors Humans Influenza virus Lentivirus - genetics Ligands Macrophages - cytology Macrophages - drug effects Macrophages - immunology Macrophages - metabolism Mass spectrometry Medical research Molecular Sequence Data Orthomyxoviridae - immunology Polypeptides Proprotein Convertases - genetics Proprotein Convertases - immunology Proprotein Convertases - metabolism Protein Processing, Post-Translational Protein Structure, Tertiary Quinolines - pharmacology Signal Transduction Toll-Like Receptor 7 - genetics Toll-Like Receptor 7 - immunology Toll-Like Receptor 7 - metabolism |
| title | Processing of Human Toll-like Receptor 7 by Furin-like Proprotein Convertases Is Required for Its Accumulation and Activity in Endosomes |
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