PMC:7243778 / 27661-28601 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"684","span":{"begin":370,"end":374},"obj":"Gene"},{"id":"685","span":{"begin":444,"end":448},"obj":"Gene"},{"id":"686","span":{"begin":165,"end":173},"obj":"Species"},{"id":"687","span":{"begin":177,"end":185},"obj":"Species"},{"id":"688","span":{"begin":245,"end":255},"obj":"Species"},{"id":"689","span":{"begin":281,"end":289},"obj":"Species"},{"id":"690","span":{"begin":710,"end":718},"obj":"Species"},{"id":"691","span":{"begin":832,"end":842},"obj":"Species"},{"id":"692","span":{"begin":924,"end":934},"obj":"Species"},{"id":"693","span":{"begin":83,"end":93},"obj":"Species"},{"id":"694","span":{"begin":843,"end":846},"obj":"Gene"},{"id":"695","span":{"begin":700,"end":706},"obj":"Chemical"},{"id":"696","span":{"begin":896,"end":902},"obj":"Chemical"},{"id":"697","span":{"begin":113,"end":121},"obj":"Disease"}],"attributes":[{"id":"A684","pred":"tao:has_database_id","subj":"684","obj":"Gene:8163"},{"id":"A685","pred":"tao:has_database_id","subj":"685","obj":"Gene:59272"},{"id":"A686","pred":"tao:has_database_id","subj":"686","obj":"Tax:694009"},{"id":"A687","pred":"tao:has_database_id","subj":"687","obj":"Tax:1335626"},{"id":"A688","pred":"tao:has_database_id","subj":"688","obj":"Tax:2697049"},{"id":"A689","pred":"tao:has_database_id","subj":"689","obj":"Tax:9606"},{"id":"A690","pred":"tao:has_database_id","subj":"690","obj":"Tax:694009"},{"id":"A691","pred":"tao:has_database_id","subj":"691","obj":"Tax:2697049"},{"id":"A692","pred":"tao:has_database_id","subj":"692","obj":"Tax:2697049"},{"id":"A693","pred":"tao:has_database_id","subj":"693","obj":"Tax:2697049"},{"id":"A694","pred":"tao:has_database_id","subj":"694","obj":"Gene:1636"},{"id":"A697","pred":"tao:has_database_id","subj":"697","obj":"MESH:D007239"}],"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":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T125","span":{"begin":0,"end":8},"obj":"Body_part"},{"id":"T126","span":{"begin":122,"end":128},"obj":"Body_part"},{"id":"T127","span":{"begin":320,"end":328},"obj":"Body_part"},{"id":"T128","span":{"begin":353,"end":361},"obj":"Body_part"},{"id":"T129","span":{"begin":576,"end":584},"obj":"Body_part"},{"id":"T130","span":{"begin":732,"end":740},"obj":"Body_part"}],"attributes":[{"id":"A125","pred":"fma_id","subj":"T125","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A126","pred":"fma_id","subj":"T126","obj":"http://purl.org/sig/ont/fma/fma62970"},{"id":"A127","pred":"fma_id","subj":"T127","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A128","pred":"fma_id","subj":"T128","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A129","pred":"fma_id","subj":"T129","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A130","pred":"fma_id","subj":"T130","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T121","span":{"begin":83,"end":91},"obj":"Disease"},{"id":"T122","span":{"begin":165,"end":173},"obj":"Disease"},{"id":"T123","span":{"begin":245,"end":253},"obj":"Disease"},{"id":"T124","span":{"begin":710,"end":718},"obj":"Disease"},{"id":"T125","span":{"begin":832,"end":836},"obj":"Disease"},{"id":"T126","span":{"begin":924,"end":932},"obj":"Disease"}],"attributes":[{"id":"A121","pred":"mondo_id","subj":"T121","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A122","pred":"mondo_id","subj":"T122","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A123","pred":"mondo_id","subj":"T123","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A124","pred":"mondo_id","subj":"T124","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A125","pred":"mondo_id","subj":"T125","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A126","pred":"mondo_id","subj":"T126","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T328","span":{"begin":122,"end":128},"obj":"http://purl.obolibrary.org/obo/UBERON_0001969"},{"id":"T329","span":{"begin":190,"end":191},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T330","span":{"begin":565,"end":566},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T331","span":{"begin":708,"end":709},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T332","span":{"begin":765,"end":769},"obj":"http://purl.obolibrary.org/obo/CLO_0001692"},{"id":"T333","span":{"begin":863,"end":865},"obj":"http://purl.obolibrary.org/obo/CLO_0001302"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T159","span":{"begin":677,"end":686},"obj":"Chemical"},{"id":"T160","span":{"begin":786,"end":793},"obj":"Chemical"}],"attributes":[{"id":"A159","pred":"chebi_id","subj":"T159","obj":"http://purl.obolibrary.org/obo/CHEBI_22587"},{"id":"A160","pred":"chebi_id","subj":"T160","obj":"http://purl.obolibrary.org/obo/CHEBI_53000"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"LitCovid-sentences","denotations":[{"id":"T216","span":{"begin":0,"end":51},"obj":"Sentence"},{"id":"T217","span":{"begin":52,"end":186},"obj":"Sentence"},{"id":"T218","span":{"begin":187,"end":290},"obj":"Sentence"},{"id":"T219","span":{"begin":291,"end":443},"obj":"Sentence"},{"id":"T220","span":{"begin":444,"end":535},"obj":"Sentence"},{"id":"T221","span":{"begin":536,"end":699},"obj":"Sentence"},{"id":"T222","span":{"begin":700,"end":867},"obj":"Sentence"},{"id":"T223","span":{"begin":868,"end":940},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}

{"project":"2_test","denotations":[{"id":"32450171-32065055-66454512","span":{"begin":863,"end":865},"obj":"32065055"}],"text":"Antibody response to RBD is viral species-specific. Effectively, none of the found SARS-CoV-2 antibodies nor the infected plasma cross-reacted with RBDs from either SARS-CoV or MERS-CoV. In a study, 206 monoclonal antibodies specific to the RBD SARS-CoV-2 were identified in eight patients. These mAbs are different in: antibody heavy and light chains, antibody clones, CDR3 length… which lead to different binding and neutralizing capacities. ACE2 is out-competed with almost 100% efficacity by some mAbs such as P2B-2F6 and P2C-1F11. Interestingly the latter and a moderate antibody P2C-1C10 seems to target the different epitopes, and they could be combined for synergistic antiviral effect [96]. CR3022, a SARS-CoV RBD-specific antibody, can bind strongly with a kd of 6.3 nM to an epitope on RBD that does not overlap with the SARS-Cov-2 ACE-2 binding site [34]. Despite its strong binding, CR3022 could not neutralize SARS-CoV-2 [97]."}