{"id":{"repo_id":"utswmed","oai_identifier":"oai:utswmed-ir.tdl.org:2152.5/4129"},"canonical_url":"https://search.dev.ndltd.org/etd/utswmed/oai:utswmed-ir.tdl.org:2152.5/4129","repository":{"repo_id":"utswmed","name":"University of Texas Southwestern Medical Center","base_url":"https://utswmed-ir.tdl.org/server/oai/request"},"display":{"title":"Structural Basis for the Activation of RIG-I/MAVS Antiviral Immune Signaling","abstract":"The file named "XU-DISSERTATION-2015.pdf" is the primary dissertation file. The supplemental file named "Movie 1.mp4" may be viewed individually.","abstract_html":"The file named "XU-DISSERTATION-2015.pdf" is the primary dissertation file. The supplemental file named "Movie 1.mp4" may be viewed individually.","abstract_has_math":false,"creators":["Xu, Hui"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Rice, Luke M.","Chen, Zhijian J.","Jiang, Qiu-Xing","Rosen, Michael K.","Liu, Qinghua"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2017,"date_issued":"2017-06-02T15:28:28Z","date_published":"2017-06-02T15:28:28Z","updated_at":"2026-07-24T05:52:31Z","subjects":["Adaptor Proteins, Signal Transducing","Immunity, Innate","Mitochondria","RNA, Viral"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["988778264"],"render_values":[{"text":"988778264","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152.5/4129","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Rice, Luke M.","Chen, Zhijian J.","Jiang, Qiu-Xing","Rosen, Michael K.","Liu, Qinghua"]},{"key":"dc:creator","label":"Author","values":["Xu, Hui"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2017-06-02T15:28:28Z","2015-05","2015-04-09","May 2015","2017-06-02T15:15:17Z"]},{"key":"dc:type","label":"Dc Type","values":["Thesis","text"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Adaptor Proteins, Signal Transducing","Immunity, Innate","Mitochondria","RNA, Viral"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152.5/4129","988778264"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The file named "XU-DISSERTATION-2015.pdf" is the primary dissertation file. The supplemental file named "Movie 1.mp4" may be viewed individually.","Retinoic acid inducible gene-I (RIG-I) is a key cytosolic pathogen RNA sensor that activates mitochondrial antiviral signaling protein (MAVS) to trigger rapid innate immune responses. Using RNAs of different lengths as model ligands, we showed that RIG-I oligomerized on dsRNA in an ATP hydrolysis-dependent and dsRNA length-dependent manner, which correlated with the strength of type-I interferon (IFN-I) activation. The obtained negative stain EM structure of full-length RIG-I in complex with a 5'ppp stem-loop RNA and the crystal structure of RIG-I/Ub complex elucidated a two-step oligomerization and conformational change of RIG-I for activation. RIG-I oligomers nucleate MAVS through homotypic interaction of the N-terminal caspase activation and recruitment domains (CARDs) and induce the formation of prion-like aggregates. The obtained cryoEM structure of left-handed helical filaments of MAVS CARD revealed specific interfaces between individual CARD subunits that are dictated by a combination of electrostatic and hydrophobic interactions and hydrogen bonding. Point mutations at multiple locations of these interfaces impaired filament formation and antiviral signaling. Super-resolution imaging of virus-infected cells revealed rod-shaped MAVS clusters on mitochondria. These results elucidated the structural mechanism of RIG-I activation by RNA and K63-linked ubiquitin chains as well as the activation of MAVS through polymerization, revealing a highly efficient signaling cascade for viral RNA sensing."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf","video/mp4"]},{"key":"dc:title","label":"Title","values":["Structural Basis for the Activation of RIG-I/MAVS Antiviral Immune Signaling"]}]}],"canonical_facts":{"dc:contributor":["Rice, Luke M.","Chen, Zhijian J.","Jiang, Qiu-Xing","Rosen, Michael K.","Liu, Qinghua"],"dc:creator":["Xu, Hui"],"dc:date":["2017-06-02T15:28:28Z","2015-05","2015-04-09","May 2015","2017-06-02T15:15:17Z"],"dc:description":["The file named "XU-DISSERTATION-2015.pdf" is the primary dissertation file. The supplemental file named "Movie 1.mp4" may be viewed individually.","Retinoic acid inducible gene-I (RIG-I) is a key cytosolic pathogen RNA sensor that activates mitochondrial antiviral signaling protein (MAVS) to trigger rapid innate immune responses. Using RNAs of different lengths as model ligands, we showed that RIG-I oligomerized on dsRNA in an ATP hydrolysis-dependent and dsRNA length-dependent manner, which correlated with the strength of type-I interferon (IFN-I) activation. The obtained negative stain EM structure of full-length RIG-I in complex with a 5'ppp stem-loop RNA and the crystal structure of RIG-I/Ub complex elucidated a two-step oligomerization and conformational change of RIG-I for activation. RIG-I oligomers nucleate MAVS through homotypic interaction of the N-terminal caspase activation and recruitment domains (CARDs) and induce the formation of prion-like aggregates. The obtained cryoEM structure of left-handed helical filaments of MAVS CARD revealed specific interfaces between individual CARD subunits that are dictated by a combination of electrostatic and hydrophobic interactions and hydrogen bonding. Point mutations at multiple locations of these interfaces impaired filament formation and antiviral signaling. Super-resolution imaging of virus-infected cells revealed rod-shaped MAVS clusters on mitochondria. These results elucidated the structural mechanism of RIG-I activation by RNA and K63-linked ubiquitin chains as well as the activation of MAVS through polymerization, revealing a highly efficient signaling cascade for viral RNA sensing."],"dc:format":["application/pdf","video/mp4"],"dc:identifier":["https://hdl.handle.net/2152.5/4129","988778264"],"dc:language":["en"],"dc:subject":["Adaptor Proteins, Signal Transducing","Immunity, Innate","Mitochondria","RNA, Viral"],"dc:title":["Structural Basis for the Activation of RIG-I/MAVS Antiviral Immune Signaling"],"dc:type":["Thesis","text"]},"updated_at":"2026-07-24T05:52:31Z"}