PMC:7352545 / 30060-31564 JSON TXT

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LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T114","span":{"begin":106,"end":108},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T115","span":{"begin":170,"end":172},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T116","span":{"begin":878,"end":880},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T117","span":{"begin":973,"end":975},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T118","span":{"begin":1244,"end":1246},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T119","span":{"begin":1400,"end":1402},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T120","span":{"begin":1463,"end":1465},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}

LitCovid-PD-FMA-UBERON

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T249","span":{"begin":330,"end":342},"obj":"Body_part"},{"id":"T250","span":{"begin":353,"end":361},"obj":"Body_part"},{"id":"T251","span":{"begin":575,"end":579},"obj":"Body_part"},{"id":"T252","span":{"begin":643,"end":647},"obj":"Body_part"}],"attributes":[{"id":"A249","pred":"fma_id","subj":"T249","obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"A250","pred":"fma_id","subj":"T250","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A251","pred":"fma_id","subj":"T251","obj":"http://purl.org/sig/ont/fma/fma74402"},{"id":"A252","pred":"fma_id","subj":"T252","obj":"http://purl.org/sig/ont/fma/fma74402"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T113","span":{"begin":471,"end":480},"obj":"Disease"},{"id":"T114","span":{"begin":704,"end":713},"obj":"Disease"}],"attributes":[{"id":"A113","pred":"mondo_id","subj":"T113","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A114","pred":"mondo_id","subj":"T114","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T398","span":{"begin":45,"end":48},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T399","span":{"begin":57,"end":60},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T400","span":{"begin":97,"end":100},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T401","span":{"begin":263,"end":264},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T402","span":{"begin":270,"end":271},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T403","span":{"begin":408,"end":415},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T404","span":{"begin":481,"end":486},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T405","span":{"begin":554,"end":555},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T406","span":{"begin":575,"end":579},"obj":"http://purl.obolibrary.org/obo/OGG_0000000002"},{"id":"T407","span":{"begin":599,"end":600},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T408","span":{"begin":615,"end":616},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T409","span":{"begin":643,"end":647},"obj":"http://purl.obolibrary.org/obo/OGG_0000000002"},{"id":"T410","span":{"begin":662,"end":665},"obj":"http://purl.obolibrary.org/obo/CLO_0001618"},{"id":"T411","span":{"begin":662,"end":665},"obj":"http://purl.obolibrary.org/obo/CLO_0001619"},{"id":"T412","span":{"begin":662,"end":665},"obj":"http://purl.obolibrary.org/obo/CLO_0001620"},{"id":"T413","span":{"begin":714,"end":719},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T414","span":{"begin":947,"end":952},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T415","span":{"begin":1060,"end":1063},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T416","span":{"begin":1079,"end":1080},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T417","span":{"begin":1120,"end":1121},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T418","span":{"begin":1150,"end":1151},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T419","span":{"begin":1218,"end":1219},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T420","span":{"begin":1335,"end":1340},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T421","span":{"begin":1487,"end":1492},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}

LitCovid-PD-CHEBI

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T298","span":{"begin":0,"end":62},"obj":"Sentence"},{"id":"T299","span":{"begin":63,"end":101},"obj":"Sentence"},{"id":"T300","span":{"begin":102,"end":226},"obj":"Sentence"},{"id":"T301","span":{"begin":227,"end":362},"obj":"Sentence"},{"id":"T302","span":{"begin":363,"end":567},"obj":"Sentence"},{"id":"T303","span":{"begin":568,"end":724},"obj":"Sentence"},{"id":"T304","span":{"begin":725,"end":900},"obj":"Sentence"},{"id":"T305","span":{"begin":901,"end":1013},"obj":"Sentence"},{"id":"T306","span":{"begin":1014,"end":1115},"obj":"Sentence"},{"id":"T307","span":{"begin":1116,"end":1259},"obj":"Sentence"},{"id":"T308","span":{"begin":1260,"end":1504},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-27185912-51943999","span":{"begin":1500,"end":1502},"obj":"27185912"},{"id":"T81483","span":{"begin":1500,"end":1502},"obj":"27185912"}],"text":"Type I HE is specific for the 9-O-acetylated SAs (9-O-Ac-SAs). Type II HE is specific for 4-O-Ac-SAs. The SA-binding shift indicates quasi-synchronous adaptations of the SA-recognition sites of the lectin and esterase domains. Type I HE monomers of β-CoV lineage A have a bimodular enzyme–lectin domain similar to cellular glycan/carbohydrate-modifying proteins. Originally, HE homologs are found in various viruses including toroviruses and orthomyxoviruses such as the influenza virus C/D and isavirus, as well as the exceptional case of β-CoV lineage A among CoVs. The HE gene was transmitted to a β-CoV lineage A progenitor via horizontal gene transfer from a 9-O-Ac-Sia–recognizing HEF, as shown in influenza virus C/D. HE acquisition and expansion occurred by cross-species transmission over HE evolution and this phenomenon reflects viral evolutionary adaptation to host SA-containing glycans. Therefore, CoV HE receptor switching precedes virus evolution driven by SA-containing glycan diversity of hosts. For instance, the BcoV HE prefers 7,9-di-O-Ac-SAs, which is also a target of the bovine torovirus HE. For a more outstanding case, such a switching event occurred in the murine CoVs for the β-CoV lineage A type switch toward O-Ac-SA recognition. In the HE specificity of murine CoVs, two different murine CoV subtypes of virus group exist with one subtype possessing the typical 9-O-Ac-SA (type I) attachment factor and the other exclusively 4-O-Ac-SA (type II) attachment virus group [56]."}