PMC:7253482 / 2300-3291
Annnotations
LitCovid-PubTator
{"project":"LitCovid-PubTator","denotations":[{"id":"103","span":{"begin":196,"end":218},"obj":"Gene"},{"id":"104","span":{"begin":220,"end":224},"obj":"Gene"},{"id":"105","span":{"begin":274,"end":305},"obj":"Gene"},{"id":"106","span":{"begin":307,"end":311},"obj":"Gene"},{"id":"107","span":{"begin":875,"end":891},"obj":"Gene"},{"id":"108","span":{"begin":893,"end":896},"obj":"Gene"},{"id":"109","span":{"begin":981,"end":984},"obj":"Gene"},{"id":"110","span":{"begin":242,"end":243},"obj":"Gene"},{"id":"111","span":{"begin":185,"end":186},"obj":"Gene"},{"id":"112","span":{"begin":534,"end":539},"obj":"Gene"},{"id":"113","span":{"begin":250,"end":260},"obj":"Species"},{"id":"114","span":{"begin":342,"end":345},"obj":"Species"},{"id":"115","span":{"begin":545,"end":555},"obj":"Species"},{"id":"116","span":{"begin":869,"end":874},"obj":"Species"},{"id":"117","span":{"begin":942,"end":953},"obj":"Species"},{"id":"118","span":{"begin":904,"end":913},"obj":"Species"},{"id":"119","span":{"begin":497,"end":512},"obj":"Chemical"},{"id":"120","span":{"begin":709,"end":716},"obj":"Chemical"},{"id":"121","span":{"begin":782,"end":788},"obj":"Chemical"},{"id":"122","span":{"begin":180,"end":184},"obj":"Disease"},{"id":"123","span":{"begin":237,"end":241},"obj":"Disease"},{"id":"124","span":{"begin":450,"end":454},"obj":"Disease"},{"id":"125","span":{"begin":459,"end":463},"obj":"Disease"}],"attributes":[{"id":"A103","pred":"tao:has_database_id","subj":"103","obj":"Gene:1803"},{"id":"A104","pred":"tao:has_database_id","subj":"104","obj":"Gene:1803"},{"id":"A105","pred":"tao:has_database_id","subj":"105","obj":"Gene:59272"},{"id":"A106","pred":"tao:has_database_id","subj":"106","obj":"Gene:59272"},{"id":"A107","pred":"tao:has_database_id","subj":"107","obj":"Gene:64006"},{"id":"A108","pred":"tao:has_database_id","subj":"108","obj":"Gene:64006"},{"id":"A109","pred":"tao:has_database_id","subj":"109","obj":"Gene:2995"},{"id":"A110","pred":"tao:has_database_id","subj":"110","obj":"Gene:43740568"},{"id":"A111","pred":"tao:has_database_id","subj":"111","obj":"Gene:43740568"},{"id":"A112","pred":"tao:has_database_id","subj":"112","obj":"Gene:43740568"},{"id":"A113","pred":"tao:has_database_id","subj":"113","obj":"Tax:2697049"},{"id":"A114","pred":"tao:has_database_id","subj":"114","obj":"Tax:11118"},{"id":"A115","pred":"tao:has_database_id","subj":"115","obj":"Tax:2697049"},{"id":"A116","pred":"tao:has_database_id","subj":"116","obj":"Tax:11676"},{"id":"A117","pred":"tao:has_database_id","subj":"117","obj":"Tax:11620"},{"id":"A118","pred":"tao:has_database_id","subj":"118","obj":"Tax:11320"},{"id":"A120","pred":"tao:has_database_id","subj":"120","obj":"MESH:D011134"},{"id":"A121","pred":"tao:has_database_id","subj":"121","obj":"MESH:D011134"},{"id":"A122","pred":"tao:has_database_id","subj":"122","obj":"MESH:D018352"},{"id":"A123","pred":"tao:has_database_id","subj":"123","obj":"MESH:D045169"},{"id":"A124","pred":"tao:has_database_id","subj":"124","obj":"MESH:D045169"},{"id":"A125","pred":"tao:has_database_id","subj":"125","obj":"MESH:D018352"}],"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":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-FMA-UBERON
{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T11","span":{"begin":17,"end":25},"obj":"Body_part"},{"id":"T12","span":{"begin":39,"end":43},"obj":"Body_part"},{"id":"T13","span":{"begin":114,"end":118},"obj":"Body_part"},{"id":"T14","span":{"begin":348,"end":356},"obj":"Body_part"},{"id":"T15","span":{"begin":394,"end":402},"obj":"Body_part"},{"id":"T16","span":{"begin":466,"end":479},"obj":"Body_part"},{"id":"T17","span":{"begin":620,"end":627},"obj":"Body_part"},{"id":"T18","span":{"begin":659,"end":672},"obj":"Body_part"},{"id":"T19","span":{"begin":846,"end":859},"obj":"Body_part"},{"id":"T20","span":{"begin":869,"end":872},"obj":"Body_part"},{"id":"T21","span":{"begin":884,"end":891},"obj":"Body_part"},{"id":"T22","span":{"begin":954,"end":966},"obj":"Body_part"}],"attributes":[{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma62925"},{"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/fma9825"},{"id":"A19","pred":"fma_id","subj":"T19","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-UBERON
{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T1","span":{"begin":659,"end":672},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002405"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-MONDO
{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T12","span":{"begin":237,"end":241},"obj":"Disease"},{"id":"T13","span":{"begin":250,"end":258},"obj":"Disease"},{"id":"T14","span":{"begin":250,"end":254},"obj":"Disease"},{"id":"T15","span":{"begin":450,"end":454},"obj":"Disease"},{"id":"T16","span":{"begin":545,"end":553},"obj":"Disease"},{"id":"T17","span":{"begin":545,"end":549},"obj":"Disease"},{"id":"T18","span":{"begin":904,"end":913},"obj":"Disease"}],"attributes":[{"id":"A12","pred":"mondo_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A13","pred":"mondo_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A14","pred":"mondo_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A15","pred":"mondo_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-CLO
{"project":"LitCovid-PD-CLO","denotations":[{"id":"T12","span":{"begin":39,"end":43},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T13","span":{"begin":59,"end":61},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T14","span":{"begin":66,"end":68},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T15","span":{"begin":66,"end":68},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T16","span":{"begin":114,"end":118},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T17","span":{"begin":145,"end":153},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T18","span":{"begin":176,"end":178},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T19","span":{"begin":316,"end":317},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T20","span":{"begin":659,"end":672},"obj":"http://purl.obolibrary.org/obo/UBERON_0002405"},{"id":"T21","span":{"begin":719,"end":721},"obj":"http://purl.obolibrary.org/obo/CLO_0050510"},{"id":"T22","span":{"begin":799,"end":802},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T23","span":{"begin":948,"end":953},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-CHEBI
{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T11","span":{"begin":17,"end":25},"obj":"Chemical"},{"id":"T12","span":{"begin":66,"end":68},"obj":"Chemical"},{"id":"T13","span":{"begin":274,"end":285},"obj":"Chemical"},{"id":"T14","span":{"begin":348,"end":356},"obj":"Chemical"},{"id":"T15","span":{"begin":394,"end":402},"obj":"Chemical"},{"id":"T16","span":{"begin":466,"end":479},"obj":"Chemical"},{"id":"T17","span":{"begin":620,"end":627},"obj":"Chemical"},{"id":"T18","span":{"begin":846,"end":859},"obj":"Chemical"},{"id":"T19","span":{"begin":884,"end":891},"obj":"Chemical"},{"id":"T20","span":{"begin":929,"end":931},"obj":"Chemical"},{"id":"T21","span":{"begin":954,"end":966},"obj":"Chemical"}],"attributes":[{"id":"A11","pred":"chebi_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A12","pred":"chebi_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"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_17089"},{"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_73924"},{"id":"A21","pred":"chebi_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-MedDRA
{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T1","span":{"begin":274,"end":303},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A1","pred":"meddra_id","subj":"T1","obj":"http://purl.bioontology.org/ontology/MEDDRA/10050289"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-IDO
{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T9","span":{"begin":34,"end":38},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T10","span":{"begin":39,"end":43},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T11","span":{"begin":109,"end":113},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T12","span":{"begin":114,"end":118},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T13","span":{"begin":318,"end":322},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T14","span":{"begin":570,"end":575},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T15","span":{"begin":646,"end":650},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T16","span":{"begin":696,"end":700},"obj":"http://purl.obolibrary.org/obo/IDO_0000531"},{"id":"T17","span":{"begin":948,"end":953},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-Enju
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MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-FMA
{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T11","span":{"begin":17,"end":25},"obj":"Body_part"},{"id":"T12","span":{"begin":39,"end":43},"obj":"Body_part"},{"id":"T13","span":{"begin":114,"end":118},"obj":"Body_part"},{"id":"T14","span":{"begin":348,"end":356},"obj":"Body_part"},{"id":"T15","span":{"begin":394,"end":402},"obj":"Body_part"},{"id":"T16","span":{"begin":466,"end":479},"obj":"Body_part"},{"id":"T17","span":{"begin":620,"end":627},"obj":"Body_part"},{"id":"T18","span":{"begin":659,"end":672},"obj":"Body_part"},{"id":"T19","span":{"begin":846,"end":859},"obj":"Body_part"},{"id":"T20","span":{"begin":869,"end":872},"obj":"Body_part"},{"id":"T21","span":{"begin":884,"end":891},"obj":"Body_part"},{"id":"T22","span":{"begin":954,"end":966},"obj":"Body_part"}],"attributes":[{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma9825"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma68646"},{"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/fma62925"},{"id":"A20","pred":"fma_id","subj":"T20","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma62925"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-CHEBI
{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T11","span":{"begin":17,"end":25},"obj":"Chemical"},{"id":"T12","span":{"begin":274,"end":285},"obj":"Chemical"},{"id":"T13","span":{"begin":348,"end":356},"obj":"Chemical"},{"id":"T14","span":{"begin":394,"end":402},"obj":"Chemical"},{"id":"T15","span":{"begin":466,"end":479},"obj":"Chemical"},{"id":"T16","span":{"begin":620,"end":627},"obj":"Chemical"},{"id":"T17","span":{"begin":846,"end":859},"obj":"Chemical"},{"id":"T18","span":{"begin":884,"end":891},"obj":"Chemical"},{"id":"T19","span":{"begin":954,"end":966},"obj":"Chemical"}],"attributes":[{"id":"A19","pred":"chebi_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A17","pred":"chebi_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A18","pred":"chebi_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A16","pred":"chebi_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A12","pred":"chebi_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A11","pred":"chebi_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-NCBITaxon
{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T20","span":{"begin":180,"end":184},"obj":"Species"},{"id":"T21","span":{"begin":237,"end":241},"obj":"Species"},{"id":"T22","span":{"begin":250,"end":258},"obj":"Species"},{"id":"T23","span":{"begin":250,"end":254},"obj":"Species"},{"id":"T24","span":{"begin":450,"end":454},"obj":"Species"},{"id":"T25","span":{"begin":459,"end":463},"obj":"Species"},{"id":"T26","span":{"begin":545,"end":555},"obj":"Species"},{"id":"T27","span":{"begin":545,"end":549},"obj":"Species"},{"id":"T28","span":{"begin":869,"end":874},"obj":"Species"},{"id":"T29","span":{"begin":942,"end":953},"obj":"Species"},{"id":"T30","span":{"begin":976,"end":980},"obj":"Species"}],"attributes":[{"id":"A22","pred":"ncbi_taxonomy_id","subj":"T22","obj":"NCBItxid:694009"},{"id":"A30","pred":"ncbi_taxonomy_id","subj":"T30","obj":"NCBItxid:11620"},{"id":"A25","pred":"ncbi_taxonomy_id","subj":"T25","obj":"NCBItxid:1335626"},{"id":"A21","pred":"ncbi_taxonomy_id","subj":"T21","obj":"NCBItxid:694009"},{"id":"A27","pred":"ncbi_taxonomy_id","subj":"T27","obj":"NCBItxid:694009"},{"id":"A29","pred":"ncbi_taxonomy_id","subj":"T29","obj":"NCBItxid:11620"},{"id":"A20","pred":"ncbi_taxonomy_id","subj":"T20","obj":"NCBItxid:1335626"},{"id":"A23","pred":"ncbi_taxonomy_id","subj":"T23","obj":"NCBItxid:694009"},{"id":"A24","pred":"ncbi_taxonomy_id","subj":"T24","obj":"NCBItxid:694009"},{"id":"A26","pred":"ncbi_taxonomy_id","subj":"T26","obj":"NCBItxid:2697049"},{"id":"A28","pred":"ncbi_taxonomy_id","subj":"T28","obj":"NCBItxid:11676"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-sentences
{"project":"LitCovid-sample-sentences","denotations":[{"id":"T16","span":{"begin":0,"end":179},"obj":"Sentence"},{"id":"T17","span":{"begin":180,"end":341},"obj":"Sentence"},{"id":"T18","span":{"begin":342,"end":576},"obj":"Sentence"},{"id":"T19","span":{"begin":577,"end":722},"obj":"Sentence"},{"id":"T20","span":{"begin":723,"end":991},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-UBERON
{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T1","span":{"begin":659,"end":672},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002405"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-MONDO
{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T12","span":{"begin":237,"end":241},"obj":"Disease"},{"id":"T13","span":{"begin":250,"end":258},"obj":"Disease"},{"id":"T14","span":{"begin":250,"end":254},"obj":"Disease"},{"id":"T15","span":{"begin":450,"end":454},"obj":"Disease"},{"id":"T16","span":{"begin":545,"end":555},"obj":"Disease"},{"id":"T17","span":{"begin":545,"end":549},"obj":"Disease"},{"id":"T18","span":{"begin":904,"end":913},"obj":"Disease"}],"attributes":[{"id":"A12","pred":"mondo_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A17","pred":"mondo_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A18","pred":"mondo_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/MONDO_0005812"},{"id":"A14","pred":"mondo_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A16","pred":"mondo_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A13","pred":"mondo_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A15","pred":"mondo_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-Pubtator
{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"122","span":{"begin":180,"end":184},"obj":"Disease"},{"id":"111","span":{"begin":185,"end":186},"obj":"Gene"},{"id":"103","span":{"begin":196,"end":218},"obj":"Gene"},{"id":"104","span":{"begin":220,"end":224},"obj":"Gene"},{"id":"123","span":{"begin":237,"end":241},"obj":"Disease"},{"id":"110","span":{"begin":242,"end":243},"obj":"Gene"},{"id":"113","span":{"begin":250,"end":260},"obj":"Species"},{"id":"105","span":{"begin":274,"end":305},"obj":"Gene"},{"id":"106","span":{"begin":307,"end":311},"obj":"Gene"},{"id":"114","span":{"begin":342,"end":345},"obj":"Species"},{"id":"124","span":{"begin":450,"end":454},"obj":"Disease"},{"id":"125","span":{"begin":459,"end":463},"obj":"Disease"},{"id":"119","span":{"begin":497,"end":512},"obj":"Chemical"},{"id":"112","span":{"begin":534,"end":539},"obj":"Gene"},{"id":"115","span":{"begin":545,"end":555},"obj":"Species"},{"id":"120","span":{"begin":709,"end":716},"obj":"Chemical"},{"id":"121","span":{"begin":782,"end":788},"obj":"Chemical"},{"id":"116","span":{"begin":869,"end":874},"obj":"Species"},{"id":"107","span":{"begin":875,"end":891},"obj":"Gene"},{"id":"108","span":{"begin":893,"end":896},"obj":"Gene"},{"id":"118","span":{"begin":904,"end":913},"obj":"Species"},{"id":"117","span":{"begin":942,"end":953},"obj":"Species"},{"id":"109","span":{"begin":981,"end":984},"obj":"Gene"}],"attributes":[{"id":"A110","pred":"pubann:denotes","subj":"110","obj":"Gene:43740568"},{"id":"A124","pred":"pubann:denotes","subj":"124","obj":"MESH:D045169"},{"id":"A123","pred":"pubann:denotes","subj":"123","obj":"MESH:D045169"},{"id":"A109","pred":"pubann:denotes","subj":"109","obj":"Gene:2995"},{"id":"A115","pred":"pubann:denotes","subj":"115","obj":"Tax:2697049"},{"id":"A117","pred":"pubann:denotes","subj":"117","obj":"Tax:11620"},{"id":"A112","pred":"pubann:denotes","subj":"112","obj":"Gene:43740568"},{"id":"A121","pred":"pubann:denotes","subj":"121","obj":"MESH:D011134"},{"id":"A120","pred":"pubann:denotes","subj":"120","obj":"MESH:D011134"},{"id":"A122","pred":"pubann:denotes","subj":"122","obj":"MESH:D018352"},{"id":"A103","pred":"pubann:denotes","subj":"103","obj":"Gene:1803"},{"id":"A118","pred":"pubann:denotes","subj":"118","obj":"Tax:11320"},{"id":"A105","pred":"pubann:denotes","subj":"105","obj":"Gene:59272"},{"id":"A113","pred":"pubann:denotes","subj":"113","obj":"Tax:2697049"},{"id":"A108","pred":"pubann:denotes","subj":"108","obj":"Gene:64006"},{"id":"A104","pred":"pubann:denotes","subj":"104","obj":"Gene:1803"},{"id":"A114","pred":"pubann:denotes","subj":"114","obj":"Tax:11118"},{"id":"A125","pred":"pubann:denotes","subj":"125","obj":"MESH:D018352"},{"id":"A107","pred":"pubann:denotes","subj":"107","obj":"Gene:64006"},{"id":"A106","pred":"pubann:denotes","subj":"106","obj":"Gene:59272"},{"id":"A116","pred":"pubann:denotes","subj":"116","obj":"Tax:11676"},{"id":"A111","pred":"pubann:denotes","subj":"111","obj":"Gene:43740568"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-UniProt
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trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-PD-GO-BP-0
{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T11","span":{"begin":145,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T12","span":{"begin":742,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0020012"},{"id":"T13","span":{"begin":742,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0051805"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sample-GO-BP
{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T10","span":{"begin":145,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T11","span":{"begin":742,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0042783"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-PD-GO-BP
{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T11","span":{"begin":145,"end":160},"obj":"http://purl.obolibrary.org/obo/GO_0061025"},{"id":"T12","span":{"begin":742,"end":756},"obj":"http://purl.obolibrary.org/obo/GO_0042783"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}
LitCovid-sentences
{"project":"LitCovid-sentences","denotations":[{"id":"T16","span":{"begin":0,"end":179},"obj":"Sentence"},{"id":"T17","span":{"begin":180,"end":341},"obj":"Sentence"},{"id":"T18","span":{"begin":342,"end":576},"obj":"Sentence"},{"id":"T19","span":{"begin":577,"end":722},"obj":"Sentence"},{"id":"T20","span":{"begin":723,"end":991},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"These trimeric S proteins mediate host-cell entry with the S1 and S2 subunits responsible for binding to the host-cell receptor and facilitating membrane fusion, respectively9–11. MERS S binds to dipeptidyl-peptidase 4 (DPP4)12, whereas SARS S13 and SARS-CoV-214,15 utilize angiotensin-converting enzyme 2 (ACE2) as a host cellular receptor. CoV S proteins are the largest class I viral fusion proteins known9, and are extensively glycosylated, with SARS and MERS S glycoproteins both encoding 69 N-linked glycan sequons per trimeric spike with SARS-CoV-2 containing 66 sites. These modifications often mask immunogenic protein epitopes from the host humoral immune system by occluding them with host-derived glycans16–18. This phenomenon of immune evasion by molecular mimicry and glycan shielding has been well characterised across other viral glycoproteins, such as HIV-1 envelope protein (Env)19–21, influenza hemagglutinin (HA)22,23 and Lassa virus glycoprotein complex (LASV GPC)24–26."}