PMC:7199903 / 14195-15028 JSONTXT

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T5","span":{"begin":97,"end":104},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T6","span":{"begin":170,"end":177},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T75","span":{"begin":68,"end":71},"obj":"Body_part"},{"id":"T76","span":{"begin":97,"end":104},"obj":"Body_part"},{"id":"T77","span":{"begin":130,"end":137},"obj":"Body_part"},{"id":"T78","span":{"begin":170,"end":177},"obj":"Body_part"},{"id":"T79","span":{"begin":361,"end":369},"obj":"Body_part"}],"attributes":[{"id":"A75","pred":"fma_id","subj":"T75","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A76","pred":"fma_id","subj":"T76","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A77","pred":"fma_id","subj":"T77","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A78","pred":"fma_id","subj":"T78","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A79","pred":"fma_id","subj":"T79","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T50","span":{"begin":334,"end":342},"obj":"Disease"},{"id":"T51","span":{"begin":348,"end":356},"obj":"Disease"},{"id":"T52","span":{"begin":461,"end":469},"obj":"Disease"}],"attributes":[{"id":"A50","pred":"mondo_id","subj":"T50","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A51","pred":"mondo_id","subj":"T51","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A52","pred":"mondo_id","subj":"T52","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T85","span":{"begin":115,"end":117},"obj":"http://purl.obolibrary.org/obo/CLO_0050507"},{"id":"T86","span":{"begin":223,"end":225},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T87","span":{"begin":283,"end":291},"obj":"http://purl.obolibrary.org/obo/CLO_0009898"},{"id":"T88","span":{"begin":308,"end":311},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T147","span":{"begin":97,"end":104},"obj":"Chemical"},{"id":"T148","span":{"begin":130,"end":137},"obj":"Chemical"},{"id":"T149","span":{"begin":170,"end":177},"obj":"Chemical"},{"id":"T150","span":{"begin":361,"end":369},"obj":"Chemical"},{"id":"T151","span":{"begin":729,"end":731},"obj":"Chemical"}],"attributes":[{"id":"A147","pred":"chebi_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/CHEBI_37684"},{"id":"A148","pred":"chebi_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A149","pred":"chebi_id","subj":"T149","obj":"http://purl.obolibrary.org/obo/CHEBI_37684"},{"id":"A150","pred":"chebi_id","subj":"T150","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A151","pred":"chebi_id","subj":"T151","obj":"http://purl.obolibrary.org/obo/CHEBI_29401"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T64","span":{"begin":375,"end":379},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"},{"id":"T65","span":{"begin":706,"end":711},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

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Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T77","span":{"begin":170,"end":177},"obj":"Body_part"},{"id":"T78","span":{"begin":361,"end":369},"obj":"Body_part"},{"id":"T74","span":{"begin":68,"end":71},"obj":"Body_part"},{"id":"T75","span":{"begin":97,"end":104},"obj":"Body_part"},{"id":"T76","span":{"begin":130,"end":137},"obj":"Body_part"}],"attributes":[{"id":"A74","pred":"fma_id","subj":"T74","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A75","pred":"fma_id","subj":"T75","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A76","pred":"fma_id","subj":"T76","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A77","pred":"fma_id","subj":"T77","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A78","pred":"fma_id","subj":"T78","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T112","span":{"begin":97,"end":104},"obj":"Chemical"},{"id":"T113","span":{"begin":130,"end":137},"obj":"Chemical"},{"id":"T114","span":{"begin":170,"end":177},"obj":"Chemical"},{"id":"T115","span":{"begin":361,"end":369},"obj":"Chemical"}],"attributes":[{"id":"A112","pred":"chebi_id","subj":"T112","obj":"http://purl.obolibrary.org/obo/CHEBI_37684"},{"id":"A113","pred":"chebi_id","subj":"T113","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A114","pred":"chebi_id","subj":"T114","obj":"http://purl.obolibrary.org/obo/CHEBI_37684"},{"id":"A115","pred":"chebi_id","subj":"T115","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T55","span":{"begin":55,"end":59},"obj":"Species"},{"id":"T56","span":{"begin":68,"end":73},"obj":"Species"},{"id":"T57","span":{"begin":271,"end":275},"obj":"Species"},{"id":"T58","span":{"begin":334,"end":342},"obj":"Species"},{"id":"T59","span":{"begin":348,"end":358},"obj":"Species"},{"id":"T60","span":{"begin":461,"end":471},"obj":"Species"}],"attributes":[{"id":"A55","pred":"ncbi_taxonomy_id","subj":"T55","obj":"NCBItxid:11620"},{"id":"A56","pred":"ncbi_taxonomy_id","subj":"T56","obj":"NCBItxid:11676"},{"id":"A57","pred":"ncbi_taxonomy_id","subj":"T57","obj":"NCBItxid:1335626"},{"id":"A58","pred":"ncbi_taxonomy_id","subj":"T58","obj":"NCBItxid:694009"},{"id":"A59","pred":"ncbi_taxonomy_id","subj":"T59","obj":"NCBItxid:2697049"},{"id":"A60","pred":"ncbi_taxonomy_id","subj":"T60","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T93","span":{"begin":0,"end":155},"obj":"Sentence"},{"id":"T94","span":{"begin":156,"end":370},"obj":"Sentence"},{"id":"T95","span":{"begin":371,"end":595},"obj":"Sentence"},{"id":"T96","span":{"begin":596,"end":833},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T44","span":{"begin":334,"end":342},"obj":"Disease"},{"id":"T45","span":{"begin":348,"end":358},"obj":"Disease"},{"id":"T46","span":{"begin":461,"end":471},"obj":"Disease"}],"attributes":[{"id":"A44","pred":"mondo_id","subj":"T44","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A45","pred":"mondo_id","subj":"T45","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A46","pred":"mondo_id","subj":"T46","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"489","span":{"begin":74,"end":77},"obj":"Gene"},{"id":"490","span":{"begin":60,"end":63},"obj":"Gene"},{"id":"491","span":{"begin":472,"end":473},"obj":"Gene"},{"id":"492","span":{"begin":359,"end":360},"obj":"Gene"},{"id":"493","span":{"begin":68,"end":73},"obj":"Species"},{"id":"494","span":{"begin":271,"end":280},"obj":"Species"},{"id":"495","span":{"begin":334,"end":342},"obj":"Species"},{"id":"496","span":{"begin":348,"end":358},"obj":"Species"},{"id":"497","span":{"begin":461,"end":471},"obj":"Species"},{"id":"498","span":{"begin":499,"end":512},"obj":"Species"},{"id":"499","span":{"begin":55,"end":59},"obj":"Species"},{"id":"500","span":{"begin":13,"end":19},"obj":"Chemical"},{"id":"501","span":{"begin":97,"end":104},"obj":"Chemical"},{"id":"502","span":{"begin":170,"end":177},"obj":"Chemical"},{"id":"503","span":{"begin":444,"end":450},"obj":"Chemical"},{"id":"504","span":{"begin":576,"end":582},"obj":"Chemical"},{"id":"505","span":{"begin":656,"end":662},"obj":"Chemical"},{"id":"506","span":{"begin":663,"end":669},"obj":"Chemical"},{"id":"507","span":{"begin":237,"end":269},"obj":"Disease"}],"attributes":[{"id":"A490","pred":"pubann:denotes","subj":"490","obj":"Gene:2995"},{"id":"A498","pred":"pubann:denotes","subj":"498","obj":"Tax:11118"},{"id":"A503","pred":"pubann:denotes","subj":"503","obj":"MESH:D011134"},{"id":"A497","pred":"pubann:denotes","subj":"497","obj":"Tax:2697049"},{"id":"A496","pred":"pubann:denotes","subj":"496","obj":"Tax:2697049"},{"id":"A489","pred":"pubann:denotes","subj":"489","obj":"Gene:100616444"},{"id":"A493","pred":"pubann:denotes","subj":"493","obj":"Tax:11676"},{"id":"A499","pred":"pubann:denotes","subj":"499","obj":"Tax:11620"},{"id":"A494","pred":"pubann:denotes","subj":"494","obj":"Tax:1335626"},{"id":"A491","pred":"pubann:denotes","subj":"491","obj":"Gene:43740568"},{"id":"A504","pred":"pubann:denotes","subj":"504","obj":"MESH:D011134"},{"id":"A495","pred":"pubann:denotes","subj":"495","obj":"Tax:694009"},{"id":"A502","pred":"pubann:denotes","subj":"502","obj":"MESH:D008358"},{"id":"A501","pred":"pubann:denotes","subj":"501","obj":"MESH:D008358"},{"id":"A500","pred":"pubann:denotes","subj":"500","obj":"MESH:D011134"},{"id":"A492","pred":"pubann:denotes","subj":"492","obj":"Gene:43740568"},{"id":"A507","pred":"pubann:denotes","subj":"507","obj":"MESH:D018352"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T2324","span":{"begin":60,"end":63},"obj":"Protein"},{"id":"T2325","span":{"begin":74,"end":77},"obj":"Protein"},{"id":"T2326","span":{"begin":359,"end":369},"obj":"Protein"}],"attributes":[{"id":"A2324","pred":"uniprot_id","subj":"T2324","obj":"https://www.uniprot.org/uniprot/P03711"},{"id":"A2325","pred":"uniprot_id","subj":"T2325","obj":"https://www.uniprot.org/uniprot/C1JJY3"},{"id":"A2326","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UIP0"},{"id":"A2327","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UIN9"},{"id":"A2328","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UIN8"},{"id":"A2329","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UIN7"},{"id":"A2330","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UIN6"},{"id":"A2331","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9UBH8"},{"id":"A2332","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NRH8"},{"id":"A2333","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NRH7"},{"id":"A2334","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NRH6"},{"id":"A2335","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NRH5"},{"id":"A2336","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NRH4"},{"id":"A2337","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NPG5"},{"id":"A2338","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NPE0"},{"id":"A2339","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q9NP52"},{"id":"A2340","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q95IF9"},{"id":"A2341","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q8N5P3"},{"id":"A2342","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q8IZU6"},{"id":"A2343","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q8IZU5"},{"id":"A2344","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q8IZU4"},{"id":"A2345","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q86Z04"},{"id":"A2346","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q7YR44"},{"id":"A2347","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q7LA71"},{"id":"A2348","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q7LA70"},{"id":"A2349","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q5STD2"},{"id":"A2350","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q5SQ85"},{"id":"A2351","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q1XI16"},{"id":"A2352","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q1XI12"},{"id":"A2353","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/Q15517"},{"id":"A2354","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/O43509"},{"id":"A2355","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/O19084"},{"id":"A2356","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/B0UYZ7"},{"id":"A2357","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/B0S7V2"},{"id":"A2358","pred":"uniprot_id","subj":"T2326","obj":"https://www.uniprot.org/uniprot/A5A6L9"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T37","span":{"begin":389,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T38","span":{"begin":639,"end":652},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T39","span":{"begin":759,"end":772},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T35","span":{"begin":389,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T36","span":{"begin":639,"end":652},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T37","span":{"begin":759,"end":772},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T41","span":{"begin":389,"end":402},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T42","span":{"begin":630,"end":652},"obj":"http://purl.obolibrary.org/obo/GO_0006493"},{"id":"T43","span":{"begin":639,"end":652},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T44","span":{"begin":750,"end":772},"obj":"http://purl.obolibrary.org/obo/GO_0006493"},{"id":"T45","span":{"begin":759,"end":772},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sample-Glycan","denotations":[{"id":"T81","span":{"begin":97,"end":104},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"T82","span":{"begin":170,"end":177},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

{"project":"LitCovid-sentences","denotations":[{"id":"T93","span":{"begin":0,"end":155},"obj":"Sentence"},{"id":"T94","span":{"begin":156,"end":370},"obj":"Sentence"},{"id":"T95","span":{"begin":371,"end":595},"obj":"Sentence"},{"id":"T96","span":{"begin":596,"end":833},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Highly dense glycan shields, such as those observed on LASV GPC and HIV-1 Env, feature so-called mannose clusters (22, 24) on the protein surface (Fig. 4). Whereas small mannose-type clusters have been characterized on the S1 subunit of Middle East respiratory syndrome (MERS)–CoV S (10), no such phenomenon has been observed for the SARS-CoV-1 or SARS-CoV-2 S proteins. The site-specific glycosylation analysis reported here suggests that the glycan shield of SARS-CoV-2 S is consistent with other coronaviruses and similarly exhibits numerous vulnerabilities throughout the glycan shield (10). Last, we detected trace levels of O-linked glycosylation at Thr323/Ser325 (T323/S325), with over 99% of these sites unmodified (fig. S4), suggesting that O-linked glycosylation of this region is minimal when the structure is native-like."}

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