PMC:7352545 / 34872-36719 JSON TXT

Annnotations TAB JSON ListView MergeView

LitCovid_Glycan-Motif-Structure

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T147","span":{"begin":268,"end":270},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T148","span":{"begin":374,"end":376},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T149","span":{"begin":405,"end":407},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T150","span":{"begin":757,"end":759},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T151","span":{"begin":1075,"end":1077},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T152","span":{"begin":1122,"end":1124},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T153","span":{"begin":1652,"end":1654},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T154","span":{"begin":1751,"end":1753},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"6.1.2. β-Coronavirus\nIn β-CoV, HE mediates viral attachment to O-Ac-SAs and its function relies on the combined CBD and RDE domains. Most β-CoVs target 9-O-Ac-SAs (type I), but certain strains switched to alternatively targeting 4-O-Ac-SAs (type II). For example, the SA-acetylesterase enzyme in BCoVs and HCoV-OC43 is known to have hemagglutinizing activities as a type of SA-9-O-acetylesterase [8]. The SA-acetylesterase is the HE surface glycoprotein in BCoV. The three-dimensional structure of BCoV HE is similar to other viral esterases [9]. The HE gene is found only in the β-CoV genus. The acetylesterase of murine CoVs differs in its substrate binding specificity from that of BCoV and HCoV-OC43, which is specific for O-acetyl residue release from SA C-9. Murine CoVs prefer to esterize 4-O-acetyl-NeuAc [64]. The β-CoV acetylesterase destroys the receptors and this specificity is similar to that of influenza viruses. Acetylesterase activity can be inhibited by diisopropyl fluorophosphate and this agent decreases viral infection levels [65]. As deduced from the SA acetylesterase of HCoV-OC43 [8], the 9-O-Ac-SA species is a receptor binding determinant for erythrocytes and entry into cells [59]. The BCoV HE protein has dual activity of acetylesterase and HA [9]. BCoV widely agglutinates erythrocytes and purified HE only agglutinates Neu5,9Ac2-enriched erythrocytes of rats and mice. BCoV and HCoV-OC43 can agglutinate chicken erythrocytes, while purified HE cannot. In contrast to the HE protein, purified S glycoprotein can agglutinate chicken erythrocytes [52], indicating that the major HA is the S protein which acts as the major SA-binding protein. However, the role of O-Ac-SAs is not certain to be essential in receptors, and SA-binding activity may be essential only to the HE protein, but not to the S glycoprotein [54]."}

LitCovid-PD-FMA-UBERON

LitCovid-PD-MONDO

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T125","span":{"begin":112,"end":115},"obj":"Disease"},{"id":"T126","span":{"begin":910,"end":919},"obj":"Disease"},{"id":"T127","span":{"begin":1026,"end":1041},"obj":"Disease"},{"id":"T128","span":{"begin":1032,"end":1041},"obj":"Disease"}],"attributes":[{"id":"A125","pred":"mondo_id","subj":"T125","obj":"http://purl.obolibrary.org/obo/MONDO_0010564"},{"id":"A126","pred":"mondo_id","subj":"T126","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A127","pred":"mondo_id","subj":"T127","obj":"http://purl.obolibrary.org/obo/MONDO_0005108"},{"id":"A128","pred":"mondo_id","subj":"T128","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"6.1.2. β-Coronavirus\nIn β-CoV, HE mediates viral attachment to O-Ac-SAs and its function relies on the combined CBD and RDE domains. Most β-CoVs target 9-O-Ac-SAs (type I), but certain strains switched to alternatively targeting 4-O-Ac-SAs (type II). For example, the SA-acetylesterase enzyme in BCoVs and HCoV-OC43 is known to have hemagglutinizing activities as a type of SA-9-O-acetylesterase [8]. The SA-acetylesterase is the HE surface glycoprotein in BCoV. The three-dimensional structure of BCoV HE is similar to other viral esterases [9]. The HE gene is found only in the β-CoV genus. The acetylesterase of murine CoVs differs in its substrate binding specificity from that of BCoV and HCoV-OC43, which is specific for O-acetyl residue release from SA C-9. Murine CoVs prefer to esterize 4-O-acetyl-NeuAc [64]. The β-CoV acetylesterase destroys the receptors and this specificity is similar to that of influenza viruses. Acetylesterase activity can be inhibited by diisopropyl fluorophosphate and this agent decreases viral infection levels [65]. As deduced from the SA acetylesterase of HCoV-OC43 [8], the 9-O-Ac-SA species is a receptor binding determinant for erythrocytes and entry into cells [59]. The BCoV HE protein has dual activity of acetylesterase and HA [9]. BCoV widely agglutinates erythrocytes and purified HE only agglutinates Neu5,9Ac2-enriched erythrocytes of rats and mice. BCoV and HCoV-OC43 can agglutinate chicken erythrocytes, while purified HE cannot. In contrast to the HE protein, purified S glycoprotein can agglutinate chicken erythrocytes [52], indicating that the major HA is the S protein which acts as the major SA-binding protein. However, the role of O-Ac-SAs is not certain to be essential in receptors, and SA-binding activity may be essential only to the HE protein, but not to the S glycoprotein [54]."}

LitCovid-PD-CLO

LitCovid-PD-CHEBI

LitCovid-PD-GO-BP

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T57","span":{"begin":1026,"end":1041},"obj":"http://purl.obolibrary.org/obo/GO_0016032"}],"text":"6.1.2. β-Coronavirus\nIn β-CoV, HE mediates viral attachment to O-Ac-SAs and its function relies on the combined CBD and RDE domains. Most β-CoVs target 9-O-Ac-SAs (type I), but certain strains switched to alternatively targeting 4-O-Ac-SAs (type II). For example, the SA-acetylesterase enzyme in BCoVs and HCoV-OC43 is known to have hemagglutinizing activities as a type of SA-9-O-acetylesterase [8]. The SA-acetylesterase is the HE surface glycoprotein in BCoV. The three-dimensional structure of BCoV HE is similar to other viral esterases [9]. The HE gene is found only in the β-CoV genus. The acetylesterase of murine CoVs differs in its substrate binding specificity from that of BCoV and HCoV-OC43, which is specific for O-acetyl residue release from SA C-9. Murine CoVs prefer to esterize 4-O-acetyl-NeuAc [64]. The β-CoV acetylesterase destroys the receptors and this specificity is similar to that of influenza viruses. Acetylesterase activity can be inhibited by diisopropyl fluorophosphate and this agent decreases viral infection levels [65]. As deduced from the SA acetylesterase of HCoV-OC43 [8], the 9-O-Ac-SA species is a receptor binding determinant for erythrocytes and entry into cells [59]. The BCoV HE protein has dual activity of acetylesterase and HA [9]. BCoV widely agglutinates erythrocytes and purified HE only agglutinates Neu5,9Ac2-enriched erythrocytes of rats and mice. BCoV and HCoV-OC43 can agglutinate chicken erythrocytes, while purified HE cannot. In contrast to the HE protein, purified S glycoprotein can agglutinate chicken erythrocytes [52], indicating that the major HA is the S protein which acts as the major SA-binding protein. However, the role of O-Ac-SAs is not certain to be essential in receptors, and SA-binding activity may be essential only to the HE protein, but not to the S glycoprotein [54]."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T341","span":{"begin":0,"end":20},"obj":"Sentence"},{"id":"T342","span":{"begin":21,"end":132},"obj":"Sentence"},{"id":"T343","span":{"begin":133,"end":250},"obj":"Sentence"},{"id":"T344","span":{"begin":251,"end":400},"obj":"Sentence"},{"id":"T345","span":{"begin":401,"end":462},"obj":"Sentence"},{"id":"T346","span":{"begin":463,"end":546},"obj":"Sentence"},{"id":"T347","span":{"begin":547,"end":592},"obj":"Sentence"},{"id":"T348","span":{"begin":593,"end":764},"obj":"Sentence"},{"id":"T349","span":{"begin":765,"end":818},"obj":"Sentence"},{"id":"T350","span":{"begin":819,"end":928},"obj":"Sentence"},{"id":"T351","span":{"begin":929,"end":1054},"obj":"Sentence"},{"id":"T352","span":{"begin":1055,"end":1210},"obj":"Sentence"},{"id":"T353","span":{"begin":1211,"end":1278},"obj":"Sentence"},{"id":"T354","span":{"begin":1279,"end":1400},"obj":"Sentence"},{"id":"T355","span":{"begin":1401,"end":1483},"obj":"Sentence"},{"id":"T356","span":{"begin":1484,"end":1671},"obj":"Sentence"},{"id":"T357","span":{"begin":1672,"end":1847},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"6.1.2. β-Coronavirus\nIn β-CoV, HE mediates viral attachment to O-Ac-SAs and its function relies on the combined CBD and RDE domains. Most β-CoVs target 9-O-Ac-SAs (type I), but certain strains switched to alternatively targeting 4-O-Ac-SAs (type II). For example, the SA-acetylesterase enzyme in BCoVs and HCoV-OC43 is known to have hemagglutinizing activities as a type of SA-9-O-acetylesterase [8]. The SA-acetylesterase is the HE surface glycoprotein in BCoV. The three-dimensional structure of BCoV HE is similar to other viral esterases [9]. The HE gene is found only in the β-CoV genus. The acetylesterase of murine CoVs differs in its substrate binding specificity from that of BCoV and HCoV-OC43, which is specific for O-acetyl residue release from SA C-9. Murine CoVs prefer to esterize 4-O-acetyl-NeuAc [64]. The β-CoV acetylesterase destroys the receptors and this specificity is similar to that of influenza viruses. Acetylesterase activity can be inhibited by diisopropyl fluorophosphate and this agent decreases viral infection levels [65]. As deduced from the SA acetylesterase of HCoV-OC43 [8], the 9-O-Ac-SA species is a receptor binding determinant for erythrocytes and entry into cells [59]. The BCoV HE protein has dual activity of acetylesterase and HA [9]. BCoV widely agglutinates erythrocytes and purified HE only agglutinates Neu5,9Ac2-enriched erythrocytes of rats and mice. BCoV and HCoV-OC43 can agglutinate chicken erythrocytes, while purified HE cannot. In contrast to the HE protein, purified S glycoprotein can agglutinate chicken erythrocytes [52], indicating that the major HA is the S protein which acts as the major SA-binding protein. However, the role of O-Ac-SAs is not certain to be essential in receptors, and SA-binding activity may be essential only to the HE protein, but not to the S glycoprotein [54]."}

2_test

{"project":"2_test","denotations":[{"id":"32604730-3380803-51944011","span":{"begin":397,"end":398},"obj":"3380803"},{"id":"32604730-1984649-51944012","span":{"begin":543,"end":544},"obj":"1984649"},{"id":"32604730-15507445-51944013","span":{"begin":814,"end":816},"obj":"15507445"},{"id":"32604730-1642550-51944014","span":{"begin":1050,"end":1052},"obj":"1642550"},{"id":"32604730-3380803-51944015","span":{"begin":1107,"end":1108},"obj":"3380803"},{"id":"32604730-1321878-51944016","span":{"begin":1206,"end":1208},"obj":"1321878"},{"id":"32604730-1984649-51944017","span":{"begin":1275,"end":1276},"obj":"1984649"},{"id":"32604730-1920630-51944018","span":{"begin":1577,"end":1579},"obj":"1920630"},{"id":"32604730-20538854-51944019","span":{"begin":1843,"end":1845},"obj":"20538854"},{"id":"T44213","span":{"begin":397,"end":398},"obj":"3380803"},{"id":"T13264","span":{"begin":543,"end":544},"obj":"1984649"},{"id":"T44537","span":{"begin":814,"end":816},"obj":"15507445"},{"id":"T62016","span":{"begin":1050,"end":1052},"obj":"1642550"},{"id":"T99141","span":{"begin":1107,"end":1108},"obj":"3380803"},{"id":"T76354","span":{"begin":1206,"end":1208},"obj":"1321878"},{"id":"T91684","span":{"begin":1275,"end":1276},"obj":"1984649"},{"id":"T34666","span":{"begin":1577,"end":1579},"obj":"1920630"},{"id":"T90252","span":{"begin":1843,"end":1845},"obj":"20538854"}],"text":"6.1.2. β-Coronavirus\nIn β-CoV, HE mediates viral attachment to O-Ac-SAs and its function relies on the combined CBD and RDE domains. Most β-CoVs target 9-O-Ac-SAs (type I), but certain strains switched to alternatively targeting 4-O-Ac-SAs (type II). For example, the SA-acetylesterase enzyme in BCoVs and HCoV-OC43 is known to have hemagglutinizing activities as a type of SA-9-O-acetylesterase [8]. The SA-acetylesterase is the HE surface glycoprotein in BCoV. The three-dimensional structure of BCoV HE is similar to other viral esterases [9]. The HE gene is found only in the β-CoV genus. The acetylesterase of murine CoVs differs in its substrate binding specificity from that of BCoV and HCoV-OC43, which is specific for O-acetyl residue release from SA C-9. Murine CoVs prefer to esterize 4-O-acetyl-NeuAc [64]. The β-CoV acetylesterase destroys the receptors and this specificity is similar to that of influenza viruses. Acetylesterase activity can be inhibited by diisopropyl fluorophosphate and this agent decreases viral infection levels [65]. As deduced from the SA acetylesterase of HCoV-OC43 [8], the 9-O-Ac-SA species is a receptor binding determinant for erythrocytes and entry into cells [59]. The BCoV HE protein has dual activity of acetylesterase and HA [9]. BCoV widely agglutinates erythrocytes and purified HE only agglutinates Neu5,9Ac2-enriched erythrocytes of rats and mice. BCoV and HCoV-OC43 can agglutinate chicken erythrocytes, while purified HE cannot. In contrast to the HE protein, purified S glycoprotein can agglutinate chicken erythrocytes [52], indicating that the major HA is the S protein which acts as the major SA-binding protein. However, the role of O-Ac-SAs is not certain to be essential in receptors, and SA-binding activity may be essential only to the HE protein, but not to the S glycoprotein [54]."}

PMC:7352545 / 34872-36719 JSONTXT

Annnotations TAB JSON ListView MergeView

PMC:7352545 / 34872-36719 JSON TXT