PMC:7048180 / 7571-8506 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T29","span":{"begin":259,"end":267},"obj":"Body_part"},{"id":"T30","span":{"begin":583,"end":591},"obj":"Body_part"},{"id":"T31","span":{"begin":639,"end":647},"obj":"Body_part"}],"attributes":[{"id":"A29","pred":"fma_id","subj":"T29","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A30","pred":"fma_id","subj":"T30","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A31","pred":"fma_id","subj":"T31","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"Next, we expressed and purified several representative SARS-CoV-specific antibodies which have been reported to target RBD and possess potent neutralizing activities, including m396 [3], CR3014 [4], CR3022 [5], as well as a MERS-CoV-specific human monoclonal antibody m336 developed by our laboratory [15], and measured their binding ability to 2019-nCoV RBD by ELISA (Figure 1(e)). Surprisingly, we found that most of these antibodies did not show evident binding to 2019-nCoV RBD. To confirm this result, we further measured the binding kinetics using BLI. An irrelevant anti-CD40 antibody was used as a negative control. Similarly, the antibody m396, which was predicted to bind 2019-nCoV RBD (Figure 1(d)), only showed slight binding at the highest measured concentration (2.0 µM). Further studies are needed to solve the high-resolution structure of 2019-nCoV RBD and understand why it could not be recognized by these antibodies."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T43","span":{"begin":55,"end":63},"obj":"Disease"}],"attributes":[{"id":"A43","pred":"mondo_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Next, we expressed and purified several representative SARS-CoV-specific antibodies which have been reported to target RBD and possess potent neutralizing activities, including m396 [3], CR3014 [4], CR3022 [5], as well as a MERS-CoV-specific human monoclonal antibody m336 developed by our laboratory [15], and measured their binding ability to 2019-nCoV RBD by ELISA (Figure 1(e)). Surprisingly, we found that most of these antibodies did not show evident binding to 2019-nCoV RBD. To confirm this result, we further measured the binding kinetics using BLI. An irrelevant anti-CD40 antibody was used as a negative control. Similarly, the antibody m396, which was predicted to bind 2019-nCoV RBD (Figure 1(d)), only showed slight binding at the highest measured concentration (2.0 µM). Further studies are needed to solve the high-resolution structure of 2019-nCoV RBD and understand why it could not be recognized by these antibodies."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T47","span":{"begin":155,"end":165},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T48","span":{"begin":222,"end":223},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T49","span":{"begin":242,"end":247},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T50","span":{"begin":604,"end":605},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Next, we expressed and purified several representative SARS-CoV-specific antibodies which have been reported to target RBD and possess potent neutralizing activities, including m396 [3], CR3014 [4], CR3022 [5], as well as a MERS-CoV-specific human monoclonal antibody m336 developed by our laboratory [15], and measured their binding ability to 2019-nCoV RBD by ELISA (Figure 1(e)). Surprisingly, we found that most of these antibodies did not show evident binding to 2019-nCoV RBD. To confirm this result, we further measured the binding kinetics using BLI. An irrelevant anti-CD40 antibody was used as a negative control. Similarly, the antibody m396, which was predicted to bind 2019-nCoV RBD (Figure 1(d)), only showed slight binding at the highest measured concentration (2.0 µM). Further studies are needed to solve the high-resolution structure of 2019-nCoV RBD and understand why it could not be recognized by these antibodies."}

{"project":"LitCovid-sentences","denotations":[{"id":"T46","span":{"begin":0,"end":382},"obj":"Sentence"},{"id":"T47","span":{"begin":383,"end":482},"obj":"Sentence"},{"id":"T48","span":{"begin":483,"end":558},"obj":"Sentence"},{"id":"T49","span":{"begin":559,"end":623},"obj":"Sentence"},{"id":"T50","span":{"begin":624,"end":785},"obj":"Sentence"},{"id":"T51","span":{"begin":786,"end":935},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Next, we expressed and purified several representative SARS-CoV-specific antibodies which have been reported to target RBD and possess potent neutralizing activities, including m396 [3], CR3014 [4], CR3022 [5], as well as a MERS-CoV-specific human monoclonal antibody m336 developed by our laboratory [15], and measured their binding ability to 2019-nCoV RBD by ELISA (Figure 1(e)). Surprisingly, we found that most of these antibodies did not show evident binding to 2019-nCoV RBD. To confirm this result, we further measured the binding kinetics using BLI. An irrelevant anti-CD40 antibody was used as a negative control. Similarly, the antibody m396, which was predicted to bind 2019-nCoV RBD (Figure 1(d)), only showed slight binding at the highest measured concentration (2.0 µM). Further studies are needed to solve the high-resolution structure of 2019-nCoV RBD and understand why it could not be recognized by these antibodies."}

{"project":"LitCovid-PubTator","denotations":[{"id":"286","span":{"begin":578,"end":582},"obj":"Gene"},{"id":"287","span":{"begin":224,"end":232},"obj":"Species"},{"id":"288","span":{"begin":345,"end":354},"obj":"Species"},{"id":"289","span":{"begin":468,"end":477},"obj":"Species"},{"id":"290","span":{"begin":682,"end":691},"obj":"Species"},{"id":"291","span":{"begin":855,"end":864},"obj":"Species"},{"id":"292","span":{"begin":55,"end":63},"obj":"Species"},{"id":"293","span":{"begin":242,"end":247},"obj":"Species"},{"id":"294","span":{"begin":187,"end":193},"obj":"Chemical"},{"id":"295","span":{"begin":199,"end":205},"obj":"Chemical"}],"attributes":[{"id":"A286","pred":"tao:has_database_id","subj":"286","obj":"Gene:958"},{"id":"A287","pred":"tao:has_database_id","subj":"287","obj":"Tax:1335626"},{"id":"A288","pred":"tao:has_database_id","subj":"288","obj":"Tax:2697049"},{"id":"A289","pred":"tao:has_database_id","subj":"289","obj":"Tax:2697049"},{"id":"A290","pred":"tao:has_database_id","subj":"290","obj":"Tax:2697049"},{"id":"A291","pred":"tao:has_database_id","subj":"291","obj":"Tax:2697049"},{"id":"A292","pred":"tao:has_database_id","subj":"292","obj":"Tax:694009"},{"id":"A293","pred":"tao:has_database_id","subj":"293","obj":"Tax:9606"}],"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":"Next, we expressed and purified several representative SARS-CoV-specific antibodies which have been reported to target RBD and possess potent neutralizing activities, including m396 [3], CR3014 [4], CR3022 [5], as well as a MERS-CoV-specific human monoclonal antibody m336 developed by our laboratory [15], and measured their binding ability to 2019-nCoV RBD by ELISA (Figure 1(e)). Surprisingly, we found that most of these antibodies did not show evident binding to 2019-nCoV RBD. To confirm this result, we further measured the binding kinetics using BLI. An irrelevant anti-CD40 antibody was used as a negative control. Similarly, the antibody m396, which was predicted to bind 2019-nCoV RBD (Figure 1(d)), only showed slight binding at the highest measured concentration (2.0 µM). Further studies are needed to solve the high-resolution structure of 2019-nCoV RBD and understand why it could not be recognized by these antibodies."}