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    LitCovid_Glycan-Motif-Structure

    MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses.

    LitCovid-PD-FMA-UBERON

    {"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T352","span":{"begin":11,"end":23},"obj":"Body_part"},{"id":"T353","span":{"begin":49,"end":61},"obj":"Body_part"},{"id":"T354","span":{"begin":110,"end":126},"obj":"Body_part"},{"id":"T355","span":{"begin":121,"end":126},"obj":"Body_part"},{"id":"T356","span":{"begin":139,"end":151},"obj":"Body_part"},{"id":"T357","span":{"begin":309,"end":321},"obj":"Body_part"},{"id":"T358","span":{"begin":338,"end":350},"obj":"Body_part"},{"id":"T359","span":{"begin":423,"end":435},"obj":"Body_part"},{"id":"T360","span":{"begin":423,"end":427},"obj":"Body_part"},{"id":"T361","span":{"begin":556,"end":569},"obj":"Body_part"},{"id":"T362","span":{"begin":769,"end":781},"obj":"Body_part"},{"id":"T363","span":{"begin":879,"end":883},"obj":"Body_part"},{"id":"T364","span":{"begin":1022,"end":1034},"obj":"Body_part"}],"attributes":[{"id":"A352","pred":"fma_id","subj":"T352","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A353","pred":"fma_id","subj":"T353","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A354","pred":"fma_id","subj":"T354","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A355","pred":"fma_id","subj":"T355","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A356","pred":"fma_id","subj":"T356","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A357","pred":"fma_id","subj":"T357","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A358","pred":"fma_id","subj":"T358","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A359","pred":"fma_id","subj":"T359","obj":"http://purl.org/sig/ont/fma/fma67653"},{"id":"A360","pred":"fma_id","subj":"T360","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A361","pred":"fma_id","subj":"T361","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A362","pred":"fma_id","subj":"T362","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A363","pred":"fma_id","subj":"T363","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A364","pred":"fma_id","subj":"T364","obj":"http://purl.org/sig/ont/fma/fma82737"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    LitCovid-PD-MONDO

    {"project":"LitCovid-PD-MONDO","denotations":[{"id":"T146","span":{"begin":950,"end":959},"obj":"Disease"}],"attributes":[{"id":"A146","pred":"mondo_id","subj":"T146","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    LitCovid-PD-CLO

    {"project":"LitCovid-PD-CLO","denotations":[{"id":"T568","span":{"begin":43,"end":48},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T569","span":{"begin":49,"end":61},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T570","span":{"begin":75,"end":80},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T571","span":{"begin":92,"end":97},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T572","span":{"begin":110,"end":120},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T573","span":{"begin":121,"end":126},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T574","span":{"begin":214,"end":217},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T575","span":{"begin":401,"end":404},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T576","span":{"begin":423,"end":427},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T577","span":{"begin":477,"end":478},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T578","span":{"begin":502,"end":505},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T579","span":{"begin":726,"end":728},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T580","span":{"begin":738,"end":740},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T581","span":{"begin":763,"end":768},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T582","span":{"begin":769,"end":781},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T583","span":{"begin":879,"end":883},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T584","span":{"begin":942,"end":945},"obj":"http://purl.obolibrary.org/obo/CLO_0051568"},{"id":"T585","span":{"begin":972,"end":973},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    LitCovid-PD-CHEBI

    {"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T1339","span":{"begin":11,"end":23},"obj":"Chemical"},{"id":"T1340","span":{"begin":139,"end":151},"obj":"Chemical"},{"id":"T1341","span":{"begin":205,"end":213},"obj":"Chemical"},{"id":"T1342","span":{"begin":244,"end":246},"obj":"Chemical"},{"id":"T1347","span":{"begin":265,"end":267},"obj":"Chemical"},{"id":"T1352","span":{"begin":278,"end":280},"obj":"Chemical"},{"id":"T1357","span":{"begin":309,"end":321},"obj":"Chemical"},{"id":"T1358","span":{"begin":338,"end":350},"obj":"Chemical"},{"id":"T1359","span":{"begin":467,"end":469},"obj":"Chemical"},{"id":"T1364","span":{"begin":556,"end":569},"obj":"Chemical"},{"id":"T1365","span":{"begin":601,"end":603},"obj":"Chemical"},{"id":"T1370","span":{"begin":636,"end":638},"obj":"Chemical"},{"id":"T1375","span":{"begin":939,"end":941},"obj":"Chemical"},{"id":"T1377","span":{"begin":1011,"end":1013},"obj":"Chemical"},{"id":"T1382","span":{"begin":1022,"end":1034},"obj":"Chemical"},{"id":"T1383","span":{"begin":1035,"end":1042},"obj":"Chemical"}],"attributes":[{"id":"A1339","pred":"chebi_id","subj":"T1339","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A1340","pred":"chebi_id","subj":"T1340","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A1341","pred":"chebi_id","subj":"T1341","obj":"http://purl.obolibrary.org/obo/CHEBI_30884"},{"id":"A1342","pred":"chebi_id","subj":"T1342","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1343","pred":"chebi_id","subj":"T1342","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1344","pred":"chebi_id","subj":"T1342","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1345","pred":"chebi_id","subj":"T1342","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1346","pred":"chebi_id","subj":"T1342","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1347","pred":"chebi_id","subj":"T1347","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1348","pred":"chebi_id","subj":"T1347","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1349","pred":"chebi_id","subj":"T1347","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1350","pred":"chebi_id","subj":"T1347","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1351","pred":"chebi_id","subj":"T1347","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1352","pred":"chebi_id","subj":"T1352","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1353","pred":"chebi_id","subj":"T1352","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1354","pred":"chebi_id","subj":"T1352","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1355","pred":"chebi_id","subj":"T1352","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1356","pred":"chebi_id","subj":"T1352","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1357","pred":"chebi_id","subj":"T1357","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A1358","pred":"chebi_id","subj":"T1358","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A1359","pred":"chebi_id","subj":"T1359","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1360","pred":"chebi_id","subj":"T1359","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1361","pred":"chebi_id","subj":"T1359","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1362","pred":"chebi_id","subj":"T1359","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1363","pred":"chebi_id","subj":"T1359","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1364","pred":"chebi_id","subj":"T1364","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A1365","pred":"chebi_id","subj":"T1365","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1366","pred":"chebi_id","subj":"T1365","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1367","pred":"chebi_id","subj":"T1365","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1368","pred":"chebi_id","subj":"T1365","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1369","pred":"chebi_id","subj":"T1365","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1370","pred":"chebi_id","subj":"T1370","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1371","pred":"chebi_id","subj":"T1370","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1372","pred":"chebi_id","subj":"T1370","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1373","pred":"chebi_id","subj":"T1370","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1374","pred":"chebi_id","subj":"T1370","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1375","pred":"chebi_id","subj":"T1375","obj":"http://purl.obolibrary.org/obo/CHEBI_33337"},{"id":"A1376","pred":"chebi_id","subj":"T1375","obj":"http://purl.obolibrary.org/obo/CHEBI_40574"},{"id":"A1377","pred":"chebi_id","subj":"T1377","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1378","pred":"chebi_id","subj":"T1377","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1379","pred":"chebi_id","subj":"T1377","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1380","pred":"chebi_id","subj":"T1377","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1381","pred":"chebi_id","subj":"T1377","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1382","pred":"chebi_id","subj":"T1382","obj":"http://purl.obolibrary.org/obo/CHEBI_16646"},{"id":"A1383","pred":"chebi_id","subj":"T1383","obj":"http://purl.obolibrary.org/obo/CHEBI_52214"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    LitCovid-PD-GO-BP

    {"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T67","span":{"begin":821,"end":829},"obj":"http://purl.obolibrary.org/obo/GO_0015297"},{"id":"T68","span":{"begin":884,"end":891},"obj":"http://purl.obolibrary.org/obo/GO_0009606"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    LitCovid-sentences

    {"project":"LitCovid-sentences","denotations":[{"id":"T403","span":{"begin":0,"end":127},"obj":"Sentence"},{"id":"T404","span":{"begin":128,"end":277},"obj":"Sentence"},{"id":"T405","span":{"begin":278,"end":441},"obj":"Sentence"},{"id":"T406","span":{"begin":442,"end":547},"obj":"Sentence"},{"id":"T407","span":{"begin":548,"end":616},"obj":"Sentence"},{"id":"T408","span":{"begin":617,"end":900},"obj":"Sentence"},{"id":"T409","span":{"begin":901,"end":1076},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}

    2_test

    {"project":"2_test","denotations":[{"id":"32604730-29684066-51944035","span":{"begin":370,"end":372},"obj":"29684066"},{"id":"32604730-21697468-51944036","span":{"begin":437,"end":439},"obj":"21697468"},{"id":"32604730-28923942-51944037","span":{"begin":783,"end":785},"obj":"28923942"},{"id":"T81260","span":{"begin":370,"end":372},"obj":"29684066"},{"id":"T98799","span":{"begin":437,"end":439},"obj":"21697468"},{"id":"T76930","span":{"begin":783,"end":785},"obj":"28923942"}],"text":"MERS-CoV S glycoprotein can hemagglutinate human erythrocytes and mediates virus entry into human respiratory epithelial cells. MERS-CoV S glycoprotein attachment is not observed for 9-O-acetylated or 5-N-glycolyl SAs, but is observed for α2,3-SA linkage over α2,6-SA linkages. SA-binding sites of MERS-CoV S glycoprotein and HCoV-OC43 S glycoprotein are not conserved [78], although they engage α2,3-SAs on the avian host cell surface [79]. MERS-CoV recognizes α2,3-SA and to a lesser extent the α2,6-SAs and sulfated SLeX for binding preference. Thus, S glycoproteins may have independently evolved SA recognition. The acquisition of SA-binding ability of MERS-CoV S seems to be an evolutionarily recent event, because HKU4 S1 and HKU5 S1 cannot hemagglutinate human erythrocytes [75], indicating flexible evolutionary exchange allowing cross-species transmission towards host cell tropism of CoVs. In conclusion, CoV recognition of 9-O-Ac-SAs for infection is based on a conserved sequence for engagement of SA-related carbohydrate ligands across CoVs and orthomyxoviruses."}