PMC:7103735 / 37531-38809 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T126","span":{"begin":171,"end":174},"obj":"Body_part"},{"id":"T127","span":{"begin":178,"end":189},"obj":"Body_part"},{"id":"T128","span":{"begin":190,"end":193},"obj":"Body_part"},{"id":"T129","span":{"begin":245,"end":252},"obj":"Body_part"},{"id":"T130","span":{"begin":290,"end":293},"obj":"Body_part"},{"id":"T131","span":{"begin":492,"end":500},"obj":"Body_part"},{"id":"T132","span":{"begin":540,"end":543},"obj":"Body_part"},{"id":"T133","span":{"begin":605,"end":608},"obj":"Body_part"},{"id":"T134","span":{"begin":651,"end":654},"obj":"Body_part"},{"id":"T135","span":{"begin":1032,"end":1040},"obj":"Body_part"}],"attributes":[{"id":"A126","pred":"fma_id","subj":"T126","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A127","pred":"fma_id","subj":"T127","obj":"http://purl.org/sig/ont/fma/fma66835"},{"id":"A128","pred":"fma_id","subj":"T128","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A129","pred":"fma_id","subj":"T129","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A130","pred":"fma_id","subj":"T130","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A131","pred":"fma_id","subj":"T131","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A132","pred":"fma_id","subj":"T132","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A133","pred":"fma_id","subj":"T133","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A134","pred":"fma_id","subj":"T134","obj":"http://purl.org/sig/ont/fma/fma67095"},{"id":"A135","pred":"fma_id","subj":"T135","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid_AGAC","denotations":[{"id":"p59868s30","span":{"begin":381,"end":394},"obj":"Protein"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T373","span":{"begin":1070,"end":1078},"obj":"Disease"},{"id":"T374","span":{"begin":1070,"end":1074},"obj":"Disease"}],"attributes":[{"id":"A373","pred":"mondo_id","subj":"T373","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A374","pred":"mondo_id","subj":"T374","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T420","span":{"begin":67,"end":84},"obj":"http://purl.obolibrary.org/obo/PR_000024990"},{"id":"T421","span":{"begin":86,"end":103},"obj":"http://purl.obolibrary.org/obo/PR_000024990"},{"id":"T422","span":{"begin":118,"end":127},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T423","span":{"begin":276,"end":286},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T424","span":{"begin":506,"end":507},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T425","span":{"begin":552,"end":569},"obj":"http://purl.obolibrary.org/obo/PR_000024990"},{"id":"T426","span":{"begin":741,"end":746},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T427","span":{"begin":770,"end":787},"obj":"http://purl.obolibrary.org/obo/PR_000024990"},{"id":"T428","span":{"begin":854,"end":857},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9397"},{"id":"T429","span":{"begin":971,"end":972},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T430","span":{"begin":1128,"end":1145},"obj":"http://purl.obolibrary.org/obo/PR_000024990"},{"id":"T431","span":{"begin":1199,"end":1207},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T110","span":{"begin":74,"end":84},"obj":"Chemical"},{"id":"T111","span":{"begin":93,"end":103},"obj":"Chemical"},{"id":"T112","span":{"begin":245,"end":252},"obj":"Chemical"},{"id":"T113","span":{"begin":492,"end":500},"obj":"Chemical"},{"id":"T114","span":{"begin":559,"end":569},"obj":"Chemical"},{"id":"T115","span":{"begin":635,"end":654},"obj":"Chemical"},{"id":"T116","span":{"begin":656,"end":661},"obj":"Chemical"},{"id":"T117","span":{"begin":777,"end":787},"obj":"Chemical"},{"id":"T118","span":{"begin":817,"end":822},"obj":"Chemical"},{"id":"T119","span":{"begin":1032,"end":1040},"obj":"Chemical"},{"id":"T120","span":{"begin":1135,"end":1145},"obj":"Chemical"}],"attributes":[{"id":"A110","pred":"chebi_id","subj":"T110","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"},{"id":"A111","pred":"chebi_id","subj":"T111","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"},{"id":"A112","pred":"chebi_id","subj":"T112","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A113","pred":"chebi_id","subj":"T113","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A114","pred":"chebi_id","subj":"T114","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"},{"id":"A115","pred":"chebi_id","subj":"T115","obj":"http://purl.obolibrary.org/obo/CHEBI_67208"},{"id":"A116","pred":"chebi_id","subj":"T116","obj":"http://purl.obolibrary.org/obo/CHEBI_67208"},{"id":"A117","pred":"chebi_id","subj":"T117","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"},{"id":"A118","pred":"chebi_id","subj":"T118","obj":"http://purl.obolibrary.org/obo/CHEBI_67208"},{"id":"A119","pred":"chebi_id","subj":"T119","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A120","pred":"chebi_id","subj":"T120","obj":"http://purl.obolibrary.org/obo/CHEBI_52999"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T42","span":{"begin":5,"end":27},"obj":"http://purl.obolibrary.org/obo/GO_0045087"},{"id":"T43","span":{"begin":12,"end":27},"obj":"http://purl.obolibrary.org/obo/GO_0006955"},{"id":"T44","span":{"begin":86,"end":114},"obj":"http://purl.obolibrary.org/obo/GO_0032606"},{"id":"T45","span":{"begin":93,"end":114},"obj":"http://purl.obolibrary.org/obo/GO_0001816"},{"id":"T46","span":{"begin":317,"end":326},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T47","span":{"begin":341,"end":345},"obj":"http://purl.obolibrary.org/obo/GO_0008384"},{"id":"T48","span":{"begin":366,"end":380},"obj":"http://purl.obolibrary.org/obo/GO_0016310"},{"id":"T49","span":{"begin":381,"end":401},"obj":"http://purl.obolibrary.org/obo/GO_0000981"},{"id":"T50","span":{"begin":381,"end":394},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T51","span":{"begin":429,"end":442},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T52","span":{"begin":552,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0032606"},{"id":"T53","span":{"begin":559,"end":580},"obj":"http://purl.obolibrary.org/obo/GO_0001816"},{"id":"T54","span":{"begin":770,"end":798},"obj":"http://purl.obolibrary.org/obo/GO_0032606"},{"id":"T55","span":{"begin":777,"end":798},"obj":"http://purl.obolibrary.org/obo/GO_0001816"},{"id":"T56","span":{"begin":1128,"end":1156},"obj":"http://purl.obolibrary.org/obo/GO_0032606"},{"id":"T57","span":{"begin":1135,"end":1156},"obj":"http://purl.obolibrary.org/obo/GO_0001816"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-sentences","denotations":[{"id":"T317","span":{"begin":0,"end":85},"obj":"Sentence"},{"id":"T318","span":{"begin":86,"end":217},"obj":"Sentence"},{"id":"T319","span":{"begin":218,"end":448},"obj":"Sentence"},{"id":"T320","span":{"begin":449,"end":617},"obj":"Sentence"},{"id":"T321","span":{"begin":618,"end":804},"obj":"Sentence"},{"id":"T322","span":{"begin":805,"end":1003},"obj":"Sentence"},{"id":"T323","span":{"begin":1004,"end":1278},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"2_test","denotations":[{"id":"32172672-26786772-27782263","span":{"begin":444,"end":446},"obj":"26786772"},{"id":"32172672-24522921-27782264","span":{"begin":800,"end":802},"obj":"24522921"},{"id":"32172672-24522921-27782265","span":{"begin":999,"end":1001},"obj":"24522921"},{"id":"32172672-19380580-27782266","span":{"begin":1158,"end":1160},"obj":"19380580"},{"id":"32172672-27094905-27782267","span":{"begin":1161,"end":1163},"obj":"27094905"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"LitCovid-PubTator","denotations":[{"id":"1090","span":{"begin":202,"end":207},"obj":"Gene"},{"id":"1091","span":{"begin":212,"end":216},"obj":"Gene"},{"id":"1092","span":{"begin":253,"end":257},"obj":"Gene"},{"id":"1093","span":{"begin":330,"end":335},"obj":"Gene"},{"id":"1094","span":{"begin":341,"end":345},"obj":"Gene"},{"id":"1095","span":{"begin":402,"end":406},"obj":"Gene"},{"id":"1096","span":{"begin":929,"end":934},"obj":"Gene"},{"id":"1097","span":{"begin":944,"end":949},"obj":"Gene"},{"id":"1098","span":{"begin":854,"end":857},"obj":"Gene"},{"id":"1099","span":{"begin":690,"end":695},"obj":"Gene"},{"id":"1100","span":{"begin":425,"end":428},"obj":"Gene"},{"id":"1101","span":{"begin":681,"end":689},"obj":"Species"},{"id":"1102","span":{"begin":734,"end":746},"obj":"Species"},{"id":"1103","span":{"begin":858,"end":861},"obj":"Species"},{"id":"1104","span":{"begin":920,"end":928},"obj":"Species"},{"id":"1105","span":{"begin":1064,"end":1068},"obj":"Species"},{"id":"1106","span":{"begin":1070,"end":1078},"obj":"Species"},{"id":"1107","span":{"begin":1083,"end":1091},"obj":"Species"},{"id":"1108","span":{"begin":751,"end":761},"obj":"Chemical"},{"id":"1109","span":{"begin":346,"end":350},"obj":"Disease"}],"attributes":[{"id":"A1090","pred":"tao:has_database_id","subj":"1090","obj":"Gene:23586"},{"id":"A1091","pred":"tao:has_database_id","subj":"1091","obj":"Gene:64135"},{"id":"A1092","pred":"tao:has_database_id","subj":"1092","obj":"Gene:57506"},{"id":"A1093","pred":"tao:has_database_id","subj":"1093","obj":"Gene:7187"},{"id":"A1094","pred":"tao:has_database_id","subj":"1094","obj":"Gene:29110"},{"id":"A1095","pred":"tao:has_database_id","subj":"1095","obj":"Gene:3661"},{"id":"A1096","pred":"tao:has_database_id","subj":"1096","obj":"Gene:14254596"},{"id":"A1097","pred":"tao:has_database_id","subj":"1097","obj":"Gene:14254596"},{"id":"A1098","pred":"tao:has_database_id","subj":"1098","obj":"Gene:570"},{"id":"A1099","pred":"tao:has_database_id","subj":"1099","obj":"Gene:14254596"},{"id":"A1100","pred":"tao:has_database_id","subj":"1100","obj":"Gene:3439"},{"id":"A1101","pred":"tao:has_database_id","subj":"1101","obj":"Tax:1335626"},{"id":"A1102","pred":"tao:has_database_id","subj":"1102","obj":"Tax:11191"},{"id":"A1103","pred":"tao:has_database_id","subj":"1103","obj":"Tax:11118"},{"id":"A1104","pred":"tao:has_database_id","subj":"1104","obj":"Tax:1335626"},{"id":"A1105","pred":"tao:has_database_id","subj":"1105","obj":"Tax:11118"},{"id":"A1106","pred":"tao:has_database_id","subj":"1106","obj":"Tax:694009"},{"id":"A1107","pred":"tao:has_database_id","subj":"1107","obj":"Tax:1335626"},{"id":"A1108","pred":"tao:has_database_id","subj":"1108","obj":"MESH:D011070"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}

{"project":"MyTest","denotations":[{"id":"32172672-26786772-27782263","span":{"begin":444,"end":446},"obj":"26786772"},{"id":"32172672-24522921-27782264","span":{"begin":800,"end":802},"obj":"24522921"},{"id":"32172672-24522921-27782265","span":{"begin":999,"end":1001},"obj":"24522921"},{"id":"32172672-19380580-27782266","span":{"begin":1158,"end":1160},"obj":"19380580"},{"id":"32172672-27094905-27782267","span":{"begin":1161,"end":1163},"obj":"27094905"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"Host innate immune response is the first-line defence triggered by type I interferon. Type I interferon production is activated through the detection of replicating viral RNA by cytoplasmic RNA sensors RIG-I and MDA5. Oligomerization of adaptor protein MAVS is induced by the activation of RNA sensor, leading to the formation of TRAF3-TANK-TBK1/IKKϵ complex, which phosphorylates transcription factor IRF3 and drives type I IFN transcription [49]. Highly pathogenic HCoVs often encode viral proteins with a higher capability to antagonize RNA-induced type I interferon production through perturbation of RNA sensing. For one example, double-stranded RNA (dsRNA)-binding domain of MERS-CoV ORF4a is responsible for the suppression of Sendai virus- or poly (I:C)-induced type I interferon production [60]. The gain of dsRNA-binding ability is observed in bat CoV HKU5 but not HKU4, suggesting that the functional gain of MERS-CoV ORF4a and HKU5 ORF4a might be acquired at a later stage in evolution [60]. For another example, only M proteins from highly pathogenic CoVs, SARS-CoV and MERS-CoV, were reported to potently suppress type I interferon production [61,62], suggesting that the loss of this activity might have taken place during viral evolution, leading to attenuation."}