PMC:7200337 / 94716-96183 JSONTXT

{"project":"2_test","denotations":[{"id":"32505227-32155444-46575426","span":{"begin":139,"end":143},"obj":"32155444"},{"id":"T4350","span":{"begin":139,"end":143},"obj":"32155444"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T736","span":{"begin":261,"end":266},"obj":"Body_part"},{"id":"T737","span":{"begin":590,"end":598},"obj":"Body_part"},{"id":"T738","span":{"begin":767,"end":772},"obj":"Body_part"},{"id":"T739","span":{"begin":937,"end":945},"obj":"Body_part"},{"id":"T740","span":{"begin":994,"end":1002},"obj":"Body_part"}],"attributes":[{"id":"A736","pred":"fma_id","subj":"T736","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A737","pred":"fma_id","subj":"T737","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A738","pred":"fma_id","subj":"T738","obj":"http://purl.org/sig/ont/fma/fma63083"},{"id":"A739","pred":"fma_id","subj":"T739","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A740","pred":"fma_id","subj":"T740","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T98","span":{"begin":767,"end":772},"obj":"Body_part"}],"attributes":[{"id":"A98","pred":"uberon_id","subj":"T98","obj":"http://purl.obolibrary.org/obo/UBERON_0001977"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T542","span":{"begin":33,"end":41},"obj":"Disease"},{"id":"T543","span":{"begin":44,"end":53},"obj":"Disease"},{"id":"T544","span":{"begin":626,"end":634},"obj":"Disease"},{"id":"T545","span":{"begin":905,"end":913},"obj":"Disease"},{"id":"T546","span":{"begin":1011,"end":1019},"obj":"Disease"},{"id":"T547","span":{"begin":1084,"end":1092},"obj":"Disease"},{"id":"T548","span":{"begin":1207,"end":1215},"obj":"Disease"},{"id":"T549","span":{"begin":1288,"end":1296},"obj":"Disease"},{"id":"T550","span":{"begin":1406,"end":1415},"obj":"Disease"}],"attributes":[{"id":"A542","pred":"mondo_id","subj":"T542","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A543","pred":"mondo_id","subj":"T543","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A544","pred":"mondo_id","subj":"T544","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A545","pred":"mondo_id","subj":"T545","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A546","pred":"mondo_id","subj":"T546","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A547","pred":"mondo_id","subj":"T547","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A548","pred":"mondo_id","subj":"T548","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A549","pred":"mondo_id","subj":"T549","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A550","pred":"mondo_id","subj":"T550","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T974","span":{"begin":259,"end":266},"obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"T975","span":{"begin":807,"end":809},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T976","span":{"begin":903,"end":904},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T977","span":{"begin":979,"end":980},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T978","span":{"begin":1175,"end":1176},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T979","span":{"begin":1241,"end":1242},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T980","span":{"begin":1243,"end":1252},"obj":"http://purl.obolibrary.org/obo/CLO_0036932"},{"id":"T981","span":{"begin":1263,"end":1264},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T982","span":{"begin":1326,"end":1327},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T983","span":{"begin":1440,"end":1441},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T210","span":{"begin":252,"end":258},"obj":"http://purl.obolibrary.org/obo/GO_0007613"},{"id":"T211","span":{"begin":590,"end":622},"obj":"http://purl.obolibrary.org/obo/GO_0097282"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-PubTator","denotations":[{"id":"3134","span":{"begin":561,"end":565},"obj":"Gene"},{"id":"3135","span":{"begin":681,"end":685},"obj":"Gene"},{"id":"3136","span":{"begin":855,"end":859},"obj":"Gene"},{"id":"3137","span":{"begin":1114,"end":1118},"obj":"Gene"},{"id":"3138","span":{"begin":1389,"end":1391},"obj":"Gene"},{"id":"3139","span":{"begin":1377,"end":1379},"obj":"Gene"},{"id":"3140","span":{"begin":1070,"end":1072},"obj":"Gene"},{"id":"3141","span":{"begin":804,"end":806},"obj":"Gene"},{"id":"3142","span":{"begin":644,"end":646},"obj":"Gene"},{"id":"3143","span":{"begin":317,"end":319},"obj":"Gene"},{"id":"3144","span":{"begin":199,"end":201},"obj":"Gene"},{"id":"3145","span":{"begin":0,"end":8},"obj":"Species"},{"id":"3146","span":{"begin":626,"end":636},"obj":"Species"},{"id":"3147","span":{"begin":789,"end":797},"obj":"Species"},{"id":"3148","span":{"begin":905,"end":913},"obj":"Species"},{"id":"3149","span":{"begin":1011,"end":1021},"obj":"Species"},{"id":"3150","span":{"begin":1084,"end":1094},"obj":"Species"},{"id":"3151","span":{"begin":1207,"end":1217},"obj":"Species"},{"id":"3152","span":{"begin":1288,"end":1298},"obj":"Species"},{"id":"3153","span":{"begin":1380,"end":1388},"obj":"Species"},{"id":"3154","span":{"begin":328,"end":339},"obj":"Species"},{"id":"3155","span":{"begin":82,"end":86},"obj":"Chemical"},{"id":"3156","span":{"begin":215,"end":219},"obj":"Chemical"},{"id":"3157","span":{"begin":1276,"end":1279},"obj":"Chemical"},{"id":"3158","span":{"begin":33,"end":53},"obj":"Disease"},{"id":"3159","span":{"begin":1406,"end":1415},"obj":"Disease"}],"attributes":[{"id":"A3134","pred":"tao:has_database_id","subj":"3134","obj":"Gene:59272"},{"id":"A3135","pred":"tao:has_database_id","subj":"3135","obj":"Gene:59272"},{"id":"A3136","pred":"tao:has_database_id","subj":"3136","obj":"Gene:59272"},{"id":"A3137","pred":"tao:has_database_id","subj":"3137","obj":"Gene:59272"},{"id":"A3138","pred":"tao:has_database_id","subj":"3138","obj":"Gene:6999"},{"id":"A3139","pred":"tao:has_database_id","subj":"3139","obj":"Gene:6999"},{"id":"A3140","pred":"tao:has_database_id","subj":"3140","obj":"Gene:6999"},{"id":"A3141","pred":"tao:has_database_id","subj":"3141","obj":"Gene:6999"},{"id":"A3142","pred":"tao:has_database_id","subj":"3142","obj":"Gene:6999"},{"id":"A3143","pred":"tao:has_database_id","subj":"3143","obj":"Gene:6999"},{"id":"A3144","pred":"tao:has_database_id","subj":"3144","obj":"Gene:6999"},{"id":"A3145","pred":"tao:has_database_id","subj":"3145","obj":"Tax:9606"},{"id":"A3146","pred":"tao:has_database_id","subj":"3146","obj":"Tax:2697049"},{"id":"A3147","pred":"tao:has_database_id","subj":"3147","obj":"Tax:9606"},{"id":"A3148","pred":"tao:has_database_id","subj":"3148","obj":"Tax:694009"},{"id":"A3149","pred":"tao:has_database_id","subj":"3149","obj":"Tax:2697049"},{"id":"A3150","pred":"tao:has_database_id","subj":"3150","obj":"Tax:2697049"},{"id":"A3151","pred":"tao:has_database_id","subj":"3151","obj":"Tax:2697049"},{"id":"A3152","pred":"tao:has_database_id","subj":"3152","obj":"Tax:2697049"},{"id":"A3153","pred":"tao:has_database_id","subj":"3153","obj":"Tax:9606"},{"id":"A3154","pred":"tao:has_database_id","subj":"3154","obj":"Tax:575864"},{"id":"A3158","pred":"tao:has_database_id","subj":"3158","obj":"MESH:C000657245"},{"id":"A3159","pred":"tao:has_database_id","subj":"3159","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":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}

{"project":"LitCovid-sentences","denotations":[{"id":"T545","span":{"begin":0,"end":185},"obj":"Sentence"},{"id":"T546","span":{"begin":186,"end":416},"obj":"Sentence"},{"id":"T547","span":{"begin":417,"end":578},"obj":"Sentence"},{"id":"T548","span":{"begin":579,"end":698},"obj":"Sentence"},{"id":"T549","span":{"begin":699,"end":893},"obj":"Sentence"},{"id":"T550","span":{"begin":894,"end":1131},"obj":"Sentence"},{"id":"T551","span":{"begin":1132,"end":1222},"obj":"Sentence"},{"id":"T552","span":{"begin":1223,"end":1467},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Patients who have recovered from SARS-CoV-2 infection are one potential source of nAbs (Chen et al., 2020a, Ju et al., 2020, Walls et al., 2020, Wölfel et al., 2020, Yuan et al., 2020). In an effort to obtain these nAbs, scientists sorted RBD-specific memory B cells and cloned their heavy and light variable regions to express recombinant forms of the corresponding antibodies (Chen et al., 2020a, Ju et al., 2020). Four of the antibodies produced in these studies (31B5, 32D4, P2C-2F6, P2C-1F11) showed high neutralizing potential in vitro, and all inhibited ACE2-RBD binding. Successful antibody-mediated neutralization of SARS-CoV-2 seemed to be dependent on the inhibition of ACE2/RBD binding. However, Chen et al. showed that nearly all antibodies derived from serum of 26 recovered patients bound to S1 and RBD, with only three actually inhibiting ACE2/RBD binding (Chen et al., 2020a). Of note, a SARS-CoV-1-derived neutralizing antibody (47D11) (Wang et al., 2020a) and a single-chain antibody against SARS-CoV-2 (n3130) (Wu et al., 2020c) have also been shown to neutralize SARS-CoV-2 without inhibiting ACE2/RBD binding. Thus, blocking this interaction may not be a prerequisite for an effective SARS-CoV-2 nAb. The generation of a hybridoma producing a monoclonal nAb against SARS-CoV-2 provides the potential for a therapeutic Ab that can be directly administered to patients to block ongoing infection and potentially even as a prophylactic (Figure 6D)."}