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Toll-Like Receptor 11 (TLR11) Interacts with Flagellin and Profilin through Disparate Mechanisms
Toll-like receptors (TLRs) are innate immune receptors that sense a variety of pathogen-associated molecular patterns (PAMPs) by interacting with them and subsequently initiating signal transduction cascades that elicit immune responses. TLR11 has been shown to interact with two known protein PAMPs:...
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Published in: | PloS one 2016-02, Vol.11 (2), p.e0148987-e0148987 |
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description | Toll-like receptors (TLRs) are innate immune receptors that sense a variety of pathogen-associated molecular patterns (PAMPs) by interacting with them and subsequently initiating signal transduction cascades that elicit immune responses. TLR11 has been shown to interact with two known protein PAMPs: Salmonella and E. coli flagellin FliC and Toxoplasma gondii profilin-like protein. Given the highly divergent biology of these pathogens recognized by TLR11, it is unclear whether common mechanisms are used to recognize these distinct protein PAMPs. Here we show that TLR11 interacts with these two PAMPs using different receptor domains. Furthermore, TLR11 binding to flagellin and profilin exhibits differential dependency on pH and receptor ectodomain cleavage. |
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TLR11 has been shown to interact with two known protein PAMPs: Salmonella and E. coli flagellin FliC and Toxoplasma gondii profilin-like protein. Given the highly divergent biology of these pathogens recognized by TLR11, it is unclear whether common mechanisms are used to recognize these distinct protein PAMPs. Here we show that TLR11 interacts with these two PAMPs using different receptor domains. Furthermore, TLR11 binding to flagellin and profilin exhibits differential dependency on pH and receptor ectodomain cleavage.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0148987</identifier><identifier>PMID: 26859749</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Analysis ; Animals ; Biology and Life Sciences ; Blotting, Western ; Cascades ; Cathepsins - metabolism ; Cellular signal transduction ; Cloning ; Cloning, Molecular ; Deoxyribonucleic acid ; Dermatology ; DNA ; E coli ; Flagellin ; Flagellin - metabolism ; Gene expression ; HEK293 Cells ; Humans ; Immune response ; Immune system ; Immunology ; Infections ; Infectious diseases ; Ligands ; Mammals ; Medicine and Health Sciences ; Mice ; Mutagenesis ; Parasites ; Pathogens ; pH effects ; Profilin ; Profilins - metabolism ; Protein Interaction Domains and Motifs ; Proteins ; Receptors ; Recombinant Proteins ; Research and Analysis Methods ; Salmonella ; Signal transduction ; Surgeons ; Toll-like receptors ; Toll-Like Receptors - immunology ; Toxoplasma ; Toxoplasma gondii ; Western blotting</subject><ispartof>PloS one, 2016-02, Vol.11 (2), p.e0148987-e0148987</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Hatai et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2016 Hatai et al 2016 Hatai et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-5f030b2549cd7881211859b3016f9d4dd689d98efde728ea7303de92c93a8e1e3</citedby><cites>FETCH-LOGICAL-c692t-5f030b2549cd7881211859b3016f9d4dd689d98efde728ea7303de92c93a8e1e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1764135350/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1764135350?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26859749$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Blader, Ira J</contributor><creatorcontrib>Hatai, Hirotsugu</creatorcontrib><creatorcontrib>Lepelley, Alice</creatorcontrib><creatorcontrib>Zeng, Wangyong</creatorcontrib><creatorcontrib>Hayden, Matthew S</creatorcontrib><creatorcontrib>Ghosh, Sankar</creatorcontrib><title>Toll-Like Receptor 11 (TLR11) Interacts with Flagellin and Profilin through Disparate Mechanisms</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Toll-like receptors (TLRs) are innate immune receptors that sense a variety of pathogen-associated molecular patterns (PAMPs) by interacting with them and subsequently initiating signal transduction cascades that elicit immune responses. 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Furthermore, TLR11 binding to flagellin and profilin exhibits differential dependency on pH and receptor ectodomain cleavage.</description><subject>Analysis</subject><subject>Animals</subject><subject>Biology and Life Sciences</subject><subject>Blotting, Western</subject><subject>Cascades</subject><subject>Cathepsins - metabolism</subject><subject>Cellular signal transduction</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Deoxyribonucleic acid</subject><subject>Dermatology</subject><subject>DNA</subject><subject>E coli</subject><subject>Flagellin</subject><subject>Flagellin - metabolism</subject><subject>Gene expression</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Immunology</subject><subject>Infections</subject><subject>Infectious diseases</subject><subject>Ligands</subject><subject>Mammals</subject><subject>Medicine and Health Sciences</subject><subject>Mice</subject><subject>Mutagenesis</subject><subject>Parasites</subject><subject>Pathogens</subject><subject>pH effects</subject><subject>Profilin</subject><subject>Profilins - 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TLR11 has been shown to interact with two known protein PAMPs: Salmonella and E. coli flagellin FliC and Toxoplasma gondii profilin-like protein. Given the highly divergent biology of these pathogens recognized by TLR11, it is unclear whether common mechanisms are used to recognize these distinct protein PAMPs. Here we show that TLR11 interacts with these two PAMPs using different receptor domains. Furthermore, TLR11 binding to flagellin and profilin exhibits differential dependency on pH and receptor ectodomain cleavage.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26859749</pmid><doi>10.1371/journal.pone.0148987</doi><oa>free_for_read</oa></addata></record> |
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subjects | Analysis Animals Biology and Life Sciences Blotting, Western Cascades Cathepsins - metabolism Cellular signal transduction Cloning Cloning, Molecular Deoxyribonucleic acid Dermatology DNA E coli Flagellin Flagellin - metabolism Gene expression HEK293 Cells Humans Immune response Immune system Immunology Infections Infectious diseases Ligands Mammals Medicine and Health Sciences Mice Mutagenesis Parasites Pathogens pH effects Profilin Profilins - metabolism Protein Interaction Domains and Motifs Proteins Receptors Recombinant Proteins Research and Analysis Methods Salmonella Signal transduction Surgeons Toll-like receptors Toll-Like Receptors - immunology Toxoplasma Toxoplasma gondii Western blotting |
title | Toll-Like Receptor 11 (TLR11) Interacts with Flagellin and Profilin through Disparate Mechanisms |
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