PMC:7199903 / 2725-3679 JSONTXT

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{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T21","span":{"begin":333,"end":341},"obj":"Disease"}],"attributes":[{"id":"A21","pred":"mondo_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T28","span":{"begin":20,"end":23},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T29","span":{"begin":527,"end":529},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T30","span":{"begin":607,"end":610},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T17","span":{"begin":86,"end":93},"obj":"Chemical"},{"id":"T18","span":{"begin":480,"end":487},"obj":"Chemical"},{"id":"T19","span":{"begin":590,"end":597},"obj":"Chemical"},{"id":"T20","span":{"begin":820,"end":827},"obj":"Chemical"},{"id":"T21","span":{"begin":880,"end":893},"obj":"Chemical"}],"attributes":[{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A19","pred":"chebi_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A20","pred":"chebi_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A21","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

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glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T17","span":{"begin":86,"end":93},"obj":"Body_part"},{"id":"T18","span":{"begin":266,"end":274},"obj":"Body_part"},{"id":"T19","span":{"begin":590,"end":597},"obj":"Body_part"},{"id":"T20","span":{"begin":709,"end":739},"obj":"Body_part"},{"id":"T21","span":{"begin":759,"end":771},"obj":"Body_part"},{"id":"T22","span":{"begin":880,"end":893},"obj":"Body_part"}],"attributes":[{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma76577"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma84806"},{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T14","span":{"begin":86,"end":93},"obj":"Chemical"},{"id":"T15","span":{"begin":480,"end":487},"obj":"Chemical"},{"id":"T16","span":{"begin":590,"end":597},"obj":"Chemical"},{"id":"T17","span":{"begin":820,"end":827},"obj":"Chemical"},{"id":"T18","span":{"begin":880,"end":893},"obj":"Chemical"}],"attributes":[{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T19","span":{"begin":333,"end":343},"obj":"Species"}],"attributes":[{"id":"A19","pred":"ncbi_taxonomy_id","subj":"T19","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T23","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T24","span":{"begin":147,"end":290},"obj":"Sentence"},{"id":"T25","span":{"begin":291,"end":436},"obj":"Sentence"},{"id":"T26","span":{"begin":437,"end":535},"obj":"Sentence"},{"id":"T27","span":{"begin":536,"end":661},"obj":"Sentence"},{"id":"T28","span":{"begin":662,"end":781},"obj":"Sentence"},{"id":"T29","span":{"begin":782,"end":954},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T19","span":{"begin":333,"end":343},"obj":"Disease"}],"attributes":[{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"108","span":{"begin":333,"end":343},"obj":"Species"},{"id":"109","span":{"begin":634,"end":647},"obj":"Species"},{"id":"110","span":{"begin":662,"end":675},"obj":"Species"},{"id":"111","span":{"begin":402,"end":403},"obj":"Chemical"},{"id":"112","span":{"begin":480,"end":487},"obj":"Chemical"},{"id":"113","span":{"begin":820,"end":827},"obj":"Chemical"}],"attributes":[{"id":"A110","pred":"pubann:denotes","subj":"110","obj":"Tax:11118"},{"id":"A111","pred":"pubann:denotes","subj":"111","obj":"MESH:D009584"},{"id":"A109","pred":"pubann:denotes","subj":"109","obj":"Tax:11118"},{"id":"A112","pred":"pubann:denotes","subj":"112","obj":"MESH:D011134"},{"id":"A108","pred":"pubann:denotes","subj":"108","obj":"Tax:2697049"},{"id":"A113","pred":"pubann:denotes","subj":"113","obj":"MESH:D011134"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T218","span":{"begin":880,"end":893},"obj":"Protein"}],"attributes":[{"id":"A218","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q9QSP1"},{"id":"A219","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q9QJT6"},{"id":"A220","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q9JGT4"},{"id":"A221","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q9IPJ6"},{"id":"A222","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q9DIC6"},{"id":"A223","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q91DS0"},{"id":"A224","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q91C28"},{"id":"A225","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8QQA2"},{"id":"A226","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8QPE5"},{"id":"A227","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8QPE4"},{"id":"A228","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8QPE3"},{"id":"A229","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8JTH0"},{"id":"A230","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8BDV6"},{"id":"A231","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8B6J6"},{"id":"A232","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8B0I1"},{"id":"A233","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8B0H6"},{"id":"A234","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q8B0H1"},{"id":"A235","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q89669"},{"id":"A236","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q85213"},{"id":"A237","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A238","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A239","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q82020"},{"id":"A240","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q787B5"},{"id":"A241","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q77SK0"},{"id":"A242","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q77N36"},{"id":"A243","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q76G52"},{"id":"A244","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q75T09"},{"id":"A245","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q6X1D5"},{"id":"A246","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q6X1D1"},{"id":"A247","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q6TYA0"},{"id":"A248","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q6E0W7"},{"id":"A249","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q66T62"},{"id":"A250","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5VKP3"},{"id":"A251","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5VKN9"},{"id":"A252","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5K2K4"},{"id":"A253","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX93"},{"id":"A254","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX92"},{"id":"A255","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX91"},{"id":"A256","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX90"},{"id":"A257","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX89"},{"id":"A258","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX88"},{"id":"A259","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5IX87"},{"id":"A260","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q5GA86"},{"id":"A261","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q58FH1"},{"id":"A262","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q4VKV3"},{"id":"A263","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q4F900"},{"id":"A264","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q49LL3"},{"id":"A265","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q49IU2"},{"id":"A266","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q49IU1"},{"id":"A267","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q49IT9"},{"id":"A268","pred":"uniprot_id","subj":"T218","obj":"https://www.uniprot.org/uniprot/Q49IT8"},{"id":"A269","pred":"unipro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glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T12","span":{"begin":6,"end":19},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T13","span":{"begin":86,"end":101},"obj":"http://purl.obolibrary.org/obo/GO_0006457"},{"id":"T14","span":{"begin":134,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T15","span":{"begin":147,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T16","span":{"begin":215,"end":229},"obj":"http://purl.obolibrary.org/obo/GO_0020012"},{"id":"T17","span":{"begin":215,"end":229},"obj":"http://purl.obolibrary.org/obo/GO_0051805"},{"id":"T18","span":{"begin":411,"end":424},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T19","span":{"begin":548,"end":561},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T20","span":{"begin":681,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0046755"},{"id":"T21","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0007114"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T11","span":{"begin":6,"end":19},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T12","span":{"begin":86,"end":101},"obj":"http://purl.obolibrary.org/obo/GO_0006457"},{"id":"T13","span":{"begin":134,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T14","span":{"begin":147,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T15","span":{"begin":215,"end":229},"obj":"http://purl.obolibrary.org/obo/GO_0042783"},{"id":"T16","span":{"begin":411,"end":424},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T17","span":{"begin":548,"end":561},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T18","span":{"begin":681,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0046755"},{"id":"T19","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0007114"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T12","span":{"begin":6,"end":19},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T13","span":{"begin":86,"end":101},"obj":"http://purl.obolibrary.org/obo/GO_0006457"},{"id":"T14","span":{"begin":134,"end":141},"obj":"http://purl.obolibrary.org/obo/GO_0009606"},{"id":"T15","span":{"begin":147,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T16","span":{"begin":215,"end":229},"obj":"http://purl.obolibrary.org/obo/GO_0042783"},{"id":"T17","span":{"begin":402,"end":424},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T18","span":{"begin":411,"end":424},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T19","span":{"begin":548,"end":561},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T20","span":{"begin":681,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0046755"},{"id":"T21","span":{"begin":692,"end":699},"obj":"http://purl.obolibrary.org/obo/GO_0007114"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-sentences","denotations":[{"id":"T23","span":{"begin":0,"end":146},"obj":"Sentence"},{"id":"T24","span":{"begin":147,"end":290},"obj":"Sentence"},{"id":"T25","span":{"begin":291,"end":436},"obj":"Sentence"},{"id":"T26","span":{"begin":437,"end":535},"obj":"Sentence"},{"id":"T27","span":{"begin":536,"end":661},"obj":"Sentence"},{"id":"T28","span":{"begin":662,"end":781},"obj":"Sentence"},{"id":"T29","span":{"begin":782,"end":954},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}

{"project":"LitCovid-PubTator","denotations":[{"id":"108","span":{"begin":333,"end":343},"obj":"Species"},{"id":"109","span":{"begin":634,"end":647},"obj":"Species"},{"id":"110","span":{"begin":662,"end":675},"obj":"Species"},{"id":"111","span":{"begin":402,"end":403},"obj":"Chemical"},{"id":"112","span":{"begin":480,"end":487},"obj":"Chemical"},{"id":"113","span":{"begin":820,"end":827},"obj":"Chemical"}],"attributes":[{"id":"A108","pred":"tao:has_database_id","subj":"108","obj":"Tax:2697049"},{"id":"A109","pred":"tao:has_database_id","subj":"109","obj":"Tax:11118"},{"id":"A110","pred":"tao:has_database_id","subj":"110","obj":"Tax:11118"},{"id":"A111","pred":"tao:has_database_id","subj":"111","obj":"MESH:D009584"},{"id":"A112","pred":"tao:has_database_id","subj":"112","obj":"MESH:D011134"},{"id":"A113","pred":"tao:has_database_id","subj":"113","obj":"MESH:D011134"}],"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":"Viral glycosylation has wide-ranging roles in viral pathobiology, including mediating protein folding and stability and shaping viral tropism (9). Glycosylation sites are under selective pressure as they facilitate immune evasion by shielding specific epitopes from antibody neutralization. However, we note the low mutation rate of SARS-CoV-2 and that as yet, there have been no observed mutations to N-linked glycosylation sites (10). Surfaces with an unusually high density of glycans can also enable immune recognition (9, 11, 12). The role of glycosylation in camouflaging immunogenic protein epitopes has been studied for other coronaviruses (10, 13, 14). Coronaviruses form virions by budding into the lumen of endoplasmic reticulum–Golgi intermediate compartments (15, 16). However, observations of complex-type glycans on virally derived material suggests that the viral glycoproteins are subjected to Golgi-resident processing enzymes (13, 17)."}