2024
Covalent Polymer‐RNA Conjugates for Potent Activation of the RIG‐I Pathway
Palmer C, Pastora L, Kimmel B, Pagendarm H, Kwiatkowski A, Stone P, Arora K, Francini N, Fedorova O, Pyle A, Wilson J. Covalent Polymer‐RNA Conjugates for Potent Activation of the RIG‐I Pathway. Advanced Healthcare Materials 2024, 14: 2303815. PMID: 38648653, PMCID: PMC11493851, DOI: 10.1002/adhm.202303815.Peer-Reviewed Original ResearchChemical design principlesActivation of RIG-I.Retinoic acid-inducible gene ICovalent conjugationRIG-I pathwayNuclease degradationThioether linkageRIG-I.Gene IRNA ligandsElectrostatic interactionsRIG-IDevelopment of therapeuticsPotent activityOligonucleotide therapeuticsNucleaseRNAAnalog carrierNanoparticlesDrug delivery barriersConjugatePolymeric carriersImmunostimulatory activityThioethersIn vivo delivery
2019
RIPLET, and not TRIM25, is required for endogenous RIG‐I‐dependent antiviral responses
Hayman T, Hsu A, Kolesnik T, Dagley L, Willemsen J, Tate M, Baker P, Kershaw N, Kedzierski L, Webb A, Wark P, Kedzierska K, Masters S, Belz G, Binder M, Hansbro P, Nicola N, Nicholson S. RIPLET, and not TRIM25, is required for endogenous RIG‐I‐dependent antiviral responses. Immunology And Cell Biology 2019, 97: 840-852. PMID: 31335993, DOI: 10.1111/imcb.12284.Peer-Reviewed Original ResearchConceptsRetinoic acid-inducible gene IRetinoic acid-inducible gene-I signalingPattern recognition receptorsInfluenza A virusRIG-I activationIII interferonsRecognition receptorsTripartite motif-containing 25Host antiviral defenseImmune signaling cascadesSusceptible to IAV infectionIFN responseInfluenza B virusIFN-stimulated genesHost cell pattern recognition receptorsHuman cell linesUpregulation of IFN-stimulated genesRIG-I.Gene IInnate immune systemRipletAntiviral defenseRIG-ITRIM25Production of type I
2016
Structural and Mechanistic Basis for S elf versus Non‐self RNA discrimination by the Innate Immune Receptor RIG‐I
Devarkar S, Wang C, Ramanathan A, Jiang F, Miller M, Khan A, Marcotrigiano J, Patel S. Structural and Mechanistic Basis for S elf versus Non‐self RNA discrimination by the Innate Immune Receptor RIG‐I. The FASEB Journal 2016, 30 DOI: 10.1096/fasebj.30.1_supplement.592.3.Peer-Reviewed Original ResearchRIG-IM7GCap-0Cellular RNARIG-I signalingPost-transcriptional modificationsReceptor RIG-ICAP-1Cellular signaling responsesType I interferon responseNucleotide riboseRIG-I.RNA discriminationBiochemical characterizationAutoinhibitory interfaceCap structureRNA ligandsRNA selectionViral immune evasion mechanismsRNA affinityX-ray crystallographyInnate immune receptor RIG-IEnd modificationSelf-RNABlunt endStructural basis for m7G recognition and 2′-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I
Devarkar S, Wang C, Miller M, Ramanathan A, Jiang F, Khan A, Patel S, Marcotrigiano J. Structural basis for m7G recognition and 2′-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 596-601. PMID: 26733676, PMCID: PMC4725518, DOI: 10.1073/pnas.1515152113.Peer-Reviewed Original ResearchConceptsCap-0M7G capG capRetinoic acid-inducible gene ICAP-1Single-stranded RNAMechanisms of hostCapped RNAHigh-affinity bindingType I IFN responseNucleotide riboseRIG-I.Gene ICap structureRNA affinityM7GStructural basisSelf-RNARNAViral immune evasionATPase activitySignaling activityStructural insightsConformational changesDsRNA
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