Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13
Crystallographic and cryo-EM analyses using short synthetic single-stranded RNAs unveil the structural basis for recognition of bacterial 23S rRNA and vesicular stomatitis virus by Toll-like receptor 13, which triggers an immune response. Toll-like receptors (TLRs) have crucial roles in innate immun...
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| Veröffentlicht in: | Nature structural & molecular biology 2015-10, Vol.22 (10), p.782-787 |
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| creator | Song, Wen Wang, Jia Han, Zhifu Zhang, Yifan Zhang, Heqiao Wang, Weiguang Chang, Junbiao Xia, Bingshu Fan, Shilong Zhang, Dekai Wang, Jiawei Wang, Hong-Wei Chai, Jijie |
| description | Crystallographic and cryo-EM analyses using short synthetic single-stranded RNAs unveil the structural basis for recognition of bacterial 23S rRNA and vesicular stomatitis virus by Toll-like receptor 13, which triggers an immune response.
Toll-like receptors (TLRs) have crucial roles in innate immunity, functioning as pattern-recognition receptors. TLR13 recognizes a conserved sequence from bacterial 23S rRNA and then triggers an immune response. Here we report the crystal structure of the mouse TLR13 ectodomain bound by a 13-nt single-stranded (ss) RNA derived from 23S rRNA. The ssRNA induces TLR13 dimerization but assumes a stem-loop-like structure that is completely different from that in the bacterial ribosome but nevertheless is crucial for TLR13 recognition. Most of the RNA nucleotides are splayed out to make base-specific contacts with the concave surface of TLR13, and RNA-specific interactions are important to allow TLR13 to distinguish RNA from DNA. Interestingly, a viral-derived 16-nt ssRNA predicted to form a similar stem-loop-like structure also induces TLR13 activation. Together, our results reveal the structural mechanism of TLR13's sequence- and conformation-specific recognition of ssRNA. |
| doi_str_mv | 10.1038/nsmb.3080 |
| format | Article |
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Toll-like receptors (TLRs) have crucial roles in innate immunity, functioning as pattern-recognition receptors. TLR13 recognizes a conserved sequence from bacterial 23S rRNA and then triggers an immune response. Here we report the crystal structure of the mouse TLR13 ectodomain bound by a 13-nt single-stranded (ss) RNA derived from 23S rRNA. The ssRNA induces TLR13 dimerization but assumes a stem-loop-like structure that is completely different from that in the bacterial ribosome but nevertheless is crucial for TLR13 recognition. Most of the RNA nucleotides are splayed out to make base-specific contacts with the concave surface of TLR13, and RNA-specific interactions are important to allow TLR13 to distinguish RNA from DNA. Interestingly, a viral-derived 16-nt ssRNA predicted to form a similar stem-loop-like structure also induces TLR13 activation. Together, our results reveal the structural mechanism of TLR13's sequence- and conformation-specific recognition of ssRNA.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.3080</identifier><identifier>PMID: 26323037</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/250 ; 631/535 ; Animals ; Biochemistry ; Biological Microscopy ; Chromatography, Gel ; Circadian rhythm ; Circadian rhythms ; Cryoelectron Microscopy ; Crystal structure ; Crystallization ; Deoxyribonucleic acid ; Dimerization ; DNA ; Image Processing, Computer-Assisted ; Immune response ; Life Sciences ; Luciferases ; Membrane Biology ; Mice ; Microscopy, Electron, Transmission ; Models, Molecular ; Oligonucleotides - genetics ; Physiological aspects ; Protein Binding ; Protein Conformation ; Protein expression ; Protein Structure ; Real-Time Polymerase Chain Reaction ; Ribonucleic acid ; RNA ; RNA, Ribosomal, 23S - chemistry ; RNA, Ribosomal, 23S - genetics ; RNA, Ribosomal, 23S - metabolism ; Structure ; Toll-like receptors ; Toll-Like Receptors - chemistry ; Toll-Like Receptors - genetics ; Toll-Like Receptors - metabolism</subject><ispartof>Nature structural & molecular biology, 2015-10, Vol.22 (10), p.782-787</ispartof><rights>Springer Nature America, Inc. 2015</rights><rights>COPYRIGHT 2015 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Oct 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c618t-55a0403db70f246335ee871275936a0e90b798fe9b6647d4d738afee2c62b9b03</citedby><cites>FETCH-LOGICAL-c618t-55a0403db70f246335ee871275936a0e90b798fe9b6647d4d738afee2c62b9b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb.3080$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb.3080$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26323037$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Song, Wen</creatorcontrib><creatorcontrib>Wang, Jia</creatorcontrib><creatorcontrib>Han, Zhifu</creatorcontrib><creatorcontrib>Zhang, Yifan</creatorcontrib><creatorcontrib>Zhang, Heqiao</creatorcontrib><creatorcontrib>Wang, Weiguang</creatorcontrib><creatorcontrib>Chang, Junbiao</creatorcontrib><creatorcontrib>Xia, Bingshu</creatorcontrib><creatorcontrib>Fan, Shilong</creatorcontrib><creatorcontrib>Zhang, Dekai</creatorcontrib><creatorcontrib>Wang, Jiawei</creatorcontrib><creatorcontrib>Wang, Hong-Wei</creatorcontrib><creatorcontrib>Chai, Jijie</creatorcontrib><title>Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Crystallographic and cryo-EM analyses using short synthetic single-stranded RNAs unveil the structural basis for recognition of bacterial 23S rRNA and vesicular stomatitis virus by Toll-like receptor 13, which triggers an immune response.
Toll-like receptors (TLRs) have crucial roles in innate immunity, functioning as pattern-recognition receptors. TLR13 recognizes a conserved sequence from bacterial 23S rRNA and then triggers an immune response. Here we report the crystal structure of the mouse TLR13 ectodomain bound by a 13-nt single-stranded (ss) RNA derived from 23S rRNA. The ssRNA induces TLR13 dimerization but assumes a stem-loop-like structure that is completely different from that in the bacterial ribosome but nevertheless is crucial for TLR13 recognition. Most of the RNA nucleotides are splayed out to make base-specific contacts with the concave surface of TLR13, and RNA-specific interactions are important to allow TLR13 to distinguish RNA from DNA. Interestingly, a viral-derived 16-nt ssRNA predicted to form a similar stem-loop-like structure also induces TLR13 activation. Together, our results reveal the structural mechanism of TLR13's sequence- and conformation-specific recognition of ssRNA.</description><subject>631/250</subject><subject>631/535</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Chromatography, Gel</subject><subject>Circadian rhythm</subject><subject>Circadian rhythms</subject><subject>Cryoelectron Microscopy</subject><subject>Crystal structure</subject><subject>Crystallization</subject><subject>Deoxyribonucleic acid</subject><subject>Dimerization</subject><subject>DNA</subject><subject>Image Processing, Computer-Assisted</subject><subject>Immune response</subject><subject>Life Sciences</subject><subject>Luciferases</subject><subject>Membrane Biology</subject><subject>Mice</subject><subject>Microscopy, Electron, Transmission</subject><subject>Models, Molecular</subject><subject>Oligonucleotides - genetics</subject><subject>Physiological aspects</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein expression</subject><subject>Protein Structure</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA, Ribosomal, 23S - chemistry</subject><subject>RNA, Ribosomal, 23S - genetics</subject><subject>RNA, Ribosomal, 23S - metabolism</subject><subject>Structure</subject><subject>Toll-like receptors</subject><subject>Toll-Like Receptors - chemistry</subject><subject>Toll-Like Receptors - genetics</subject><subject>Toll-Like Receptors - 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Yifan</au><au>Zhang, Heqiao</au><au>Wang, Weiguang</au><au>Chang, Junbiao</au><au>Xia, Bingshu</au><au>Fan, Shilong</au><au>Zhang, Dekai</au><au>Wang, Jiawei</au><au>Wang, Hong-Wei</au><au>Chai, Jijie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2015-10-01</date><risdate>2015</risdate><volume>22</volume><issue>10</issue><spage>782</spage><epage>787</epage><pages>782-787</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Crystallographic and cryo-EM analyses using short synthetic single-stranded RNAs unveil the structural basis for recognition of bacterial 23S rRNA and vesicular stomatitis virus by Toll-like receptor 13, which triggers an immune response.
Toll-like receptors (TLRs) have crucial roles in innate immunity, functioning as pattern-recognition receptors. TLR13 recognizes a conserved sequence from bacterial 23S rRNA and then triggers an immune response. Here we report the crystal structure of the mouse TLR13 ectodomain bound by a 13-nt single-stranded (ss) RNA derived from 23S rRNA. The ssRNA induces TLR13 dimerization but assumes a stem-loop-like structure that is completely different from that in the bacterial ribosome but nevertheless is crucial for TLR13 recognition. Most of the RNA nucleotides are splayed out to make base-specific contacts with the concave surface of TLR13, and RNA-specific interactions are important to allow TLR13 to distinguish RNA from DNA. Interestingly, a viral-derived 16-nt ssRNA predicted to form a similar stem-loop-like structure also induces TLR13 activation. Together, our results reveal the structural mechanism of TLR13's sequence- and conformation-specific recognition of ssRNA.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>26323037</pmid><doi>10.1038/nsmb.3080</doi><tpages>6</tpages></addata></record> |
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| subjects | 631/250 631/535 Animals Biochemistry Biological Microscopy Chromatography, Gel Circadian rhythm Circadian rhythms Cryoelectron Microscopy Crystal structure Crystallization Deoxyribonucleic acid Dimerization DNA Image Processing, Computer-Assisted Immune response Life Sciences Luciferases Membrane Biology Mice Microscopy, Electron, Transmission Models, Molecular Oligonucleotides - genetics Physiological aspects Protein Binding Protein Conformation Protein expression Protein Structure Real-Time Polymerase Chain Reaction Ribonucleic acid RNA RNA, Ribosomal, 23S - chemistry RNA, Ribosomal, 23S - genetics RNA, Ribosomal, 23S - metabolism Structure Toll-like receptors Toll-Like Receptors - chemistry Toll-Like Receptors - genetics Toll-Like Receptors - metabolism |
| title | Structural basis for specific recognition of single-stranded RNA by Toll-like receptor 13 |
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