PMC:7219429 / 26386-27442 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T166","span":{"begin":61,"end":68},"obj":"Body_part"},{"id":"T167","span":{"begin":169,"end":174},"obj":"Body_part"},{"id":"T168","span":{"begin":372,"end":384},"obj":"Body_part"},{"id":"T169","span":{"begin":416,"end":427},"obj":"Body_part"},{"id":"T170","span":{"begin":559,"end":572},"obj":"Body_part"},{"id":"T171","span":{"begin":559,"end":563},"obj":"Body_part"},{"id":"T172","span":{"begin":675,"end":678},"obj":"Body_part"},{"id":"T173","span":{"begin":730,"end":738},"obj":"Body_part"},{"id":"T174","span":{"begin":798,"end":815},"obj":"Body_part"},{"id":"T175","span":{"begin":871,"end":878},"obj":"Body_part"},{"id":"T176","span":{"begin":949,"end":961},"obj":"Body_part"},{"id":"T177","span":{"begin":1032,"end":1037},"obj":"Body_part"}],"attributes":[{"id":"A166","pred":"fma_id","subj":"T166","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A167","pred":"fma_id","subj":"T167","obj":"http://purl.org/sig/ont/fma/fma67264"},{"id":"A168","pred":"fma_id","subj":"T168","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A169","pred":"fma_id","subj":"T169","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A170","pred":"fma_id","subj":"T170","obj":"http://purl.org/sig/ont/fma/fma63841"},{"id":"A171","pred":"fma_id","subj":"T171","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A172","pred":"fma_id","subj":"T172","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A173","pred":"fma_id","subj":"T173","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A174","pred":"fma_id","subj":"T174","obj":"http://purl.org/sig/ont/fma/fma82814"},{"id":"A175","pred":"fma_id","subj":"T175","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A176","pred":"fma_id","subj":"T176","obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"A177","pred":"fma_id","subj":"T177","obj":"http://purl.org/sig/ont/fma/fma67264"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T88","span":{"begin":50,"end":58},"obj":"Disease"},{"id":"T89","span":{"begin":230,"end":245},"obj":"Disease"},{"id":"T90","span":{"begin":236,"end":245},"obj":"Disease"},{"id":"T91","span":{"begin":635,"end":650},"obj":"Disease"},{"id":"T92","span":{"begin":641,"end":650},"obj":"Disease"},{"id":"T93","span":{"begin":837,"end":845},"obj":"Disease"}],"attributes":[{"id":"A88","pred":"mondo_id","subj":"T88","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A89","pred":"mondo_id","subj":"T89","obj":"http://purl.obolibrary.org/obo/MONDO_0005108"},{"id":"A90","pred":"mondo_id","subj":"T90","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A91","pred":"mondo_id","subj":"T91","obj":"http://purl.obolibrary.org/obo/MONDO_0005108"},{"id":"A92","pred":"mondo_id","subj":"T92","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A93","pred":"mondo_id","subj":"T93","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T246","span":{"begin":139,"end":141},"obj":"http://purl.obolibrary.org/obo/CLO_0053733"},{"id":"T247","span":{"begin":209,"end":210},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T248","span":{"begin":230,"end":235},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T249","span":{"begin":280,"end":285},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T250","span":{"begin":527,"end":528},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T251","span":{"begin":548,"end":553},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T252","span":{"begin":559,"end":563},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T253","span":{"begin":564,"end":572},"obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"T254","span":{"begin":635,"end":640},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T255","span":{"begin":748,"end":749},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T256","span":{"begin":760,"end":763},"obj":"http://purl.obolibrary.org/obo/PR_000001004"},{"id":"T257","span":{"begin":766,"end":767},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T258","span":{"begin":900,"end":907},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T259","span":{"begin":1021,"end":1028},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T502","span":{"begin":61,"end":68},"obj":"Chemical"},{"id":"T503","span":{"begin":169,"end":174},"obj":"Chemical"},{"id":"T504","span":{"begin":372,"end":384},"obj":"Chemical"},{"id":"T505","span":{"begin":416,"end":427},"obj":"Chemical"},{"id":"T506","span":{"begin":730,"end":738},"obj":"Chemical"},{"id":"T507","span":{"begin":798,"end":815},"obj":"Chemical"},{"id":"T508","span":{"begin":816,"end":825},"obj":"Chemical"},{"id":"T509","span":{"begin":871,"end":878},"obj":"Chemical"},{"id":"T510","span":{"begin":949,"end":961},"obj":"Chemical"},{"id":"T511","span":{"begin":1032,"end":1037},"obj":"Chemical"}],"attributes":[{"id":"A502","pred":"chebi_id","subj":"T502","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A503","pred":"chebi_id","subj":"T503","obj":"http://purl.obolibrary.org/obo/CHEBI_18059"},{"id":"A504","pred":"chebi_id","subj":"T504","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A505","pred":"chebi_id","subj":"T505","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A506","pred":"chebi_id","subj":"T506","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A507","pred":"chebi_id","subj":"T507","obj":"http://purl.obolibrary.org/obo/CHEBI_24402"},{"id":"A508","pred":"chebi_id","subj":"T508","obj":"http://purl.obolibrary.org/obo/CHEBI_23357"},{"id":"A509","pred":"chebi_id","subj":"T509","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A510","pred":"chebi_id","subj":"T510","obj":"http://purl.obolibrary.org/obo/CHEBI_28892"},{"id":"A511","pred":"chebi_id","subj":"T511","obj":"http://purl.obolibrary.org/obo/CHEBI_18059"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"LitCovid-sentences","denotations":[{"id":"T193","span":{"begin":0,"end":147},"obj":"Sentence"},{"id":"T194","span":{"begin":148,"end":251},"obj":"Sentence"},{"id":"T195","span":{"begin":252,"end":385},"obj":"Sentence"},{"id":"T196","span":{"begin":386,"end":521},"obj":"Sentence"},{"id":"T197","span":{"begin":522,"end":662},"obj":"Sentence"},{"id":"T198","span":{"begin":663,"end":831},"obj":"Sentence"},{"id":"T199","span":{"begin":832,"end":1056},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"LitCovid-PubTator","denotations":[{"id":"729","span":{"begin":132,"end":137},"obj":"Gene"},{"id":"730","span":{"begin":157,"end":162},"obj":"Gene"},{"id":"731","span":{"begin":362,"end":367},"obj":"Gene"},{"id":"732","span":{"begin":706,"end":711},"obj":"Gene"},{"id":"733","span":{"begin":760,"end":763},"obj":"Gene"},{"id":"734","span":{"begin":788,"end":792},"obj":"Gene"},{"id":"735","span":{"begin":484,"end":489},"obj":"Gene"},{"id":"736","span":{"begin":50,"end":60},"obj":"Species"},{"id":"737","span":{"begin":675,"end":680},"obj":"Species"},{"id":"738","span":{"begin":837,"end":847},"obj":"Species"},{"id":"739","span":{"begin":169,"end":174},"obj":"Chemical"},{"id":"740","span":{"begin":372,"end":384},"obj":"Chemical"},{"id":"741","span":{"begin":416,"end":427},"obj":"Chemical"},{"id":"742","span":{"begin":949,"end":961},"obj":"Chemical"},{"id":"743","span":{"begin":1032,"end":1037},"obj":"Chemical"},{"id":"744","span":{"begin":218,"end":245},"obj":"Disease"},{"id":"745","span":{"begin":635,"end":650},"obj":"Disease"}],"attributes":[{"id":"A729","pred":"tao:has_database_id","subj":"729","obj":"Gene:59272"},{"id":"A730","pred":"tao:has_database_id","subj":"730","obj":"Gene:59272"},{"id":"A731","pred":"tao:has_database_id","subj":"731","obj":"Gene:59272"},{"id":"A732","pred":"tao:has_database_id","subj":"732","obj":"Gene:3700"},{"id":"A733","pred":"tao:has_database_id","subj":"733","obj":"Gene:920"},{"id":"A734","pred":"tao:has_database_id","subj":"734","obj":"Gene:1234"},{"id":"A735","pred":"tao:has_database_id","subj":"735","obj":"Gene:43740568"},{"id":"A736","pred":"tao:has_database_id","subj":"736","obj":"Tax:2697049"},{"id":"A737","pred":"tao:has_database_id","subj":"737","obj":"Tax:11676"},{"id":"A738","pred":"tao:has_database_id","subj":"738","obj":"Tax:2697049"},{"id":"A739","pred":"tao:has_database_id","subj":"739","obj":"MESH:D008055"},{"id":"A740","pred":"tao:has_database_id","subj":"740","obj":"MESH:D005732"},{"id":"A741","pred":"tao:has_database_id","subj":"741","obj":"MESH:D005732"},{"id":"A742","pred":"tao:has_database_id","subj":"742","obj":"MESH:D005732"},{"id":"A743","pred":"tao:has_database_id","subj":"743","obj":"MESH:D008055"},{"id":"A744","pred":"tao:has_database_id","subj":"744","obj":"MESH:D001102"},{"id":"A745","pred":"tao:has_database_id","subj":"745","obj":"MESH:D001102"}],"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":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}

{"project":"2_test","denotations":[{"id":"32405156-32132184-48151033","span":{"begin":139,"end":141},"obj":"32132184"},{"id":"32405156-32075877-48151034","span":{"begin":143,"end":145},"obj":"32075877"},{"id":"32405156-18814896-48151035","span":{"begin":247,"end":249},"obj":"18814896"},{"id":"32405156-10233996-48151036","span":{"begin":827,"end":829},"obj":"10233996"},{"id":"32405156-18353982-48151037","span":{"begin":1052,"end":1054},"obj":"18353982"},{"id":"T12821","span":{"begin":139,"end":141},"obj":"32132184"},{"id":"T54020","span":{"begin":143,"end":145},"obj":"32075877"},{"id":"T89246","span":{"begin":247,"end":249},"obj":"18814896"},{"id":"T51159","span":{"begin":827,"end":829},"obj":"10233996"},{"id":"T64785","span":{"begin":1052,"end":1054},"obj":"18353982"}],"text":"To date, there are several structural data of the SARS-CoV-2 protein in the prefusion conformation or bound to its primary receptor ACE-2 [11, 20]. However, ACE-2 is in lipid rafts and raft disruption induces a marked decrease of virus infection [15]. Thus, it is likely that the virus interacts with the raft surface through multivalent contacts involving both ACE-2 and gangliosides. The fact that the RBD and the ganglioside-binding domain belong to distinct parts of the trimeric spike is consistent with this notion. Such a complex network of virus-host cell membrane interactions is also consistent with previously characterized virus infection strategies. Indeed, the HIV-1 fusion process driven by gp120 and gp41 envelope proteins involves a receptor (CD4), a coreceptor (chiefly CCR5) and glycosphingolipid cofactors [39]. Like SARS-CoV-2, the pentameric capsid protein of SV40, and polyoma viruses display three distinct binding sites for gangliosides, which serve as critical receptors for these non-enveloped viruses in lipid raft domains [40]."}