PMC:7205724 / 20533-21806 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"696","span":{"begin":107,"end":116},"obj":"Species"},{"id":"697","span":{"begin":117,"end":126},"obj":"Disease"},{"id":"713","span":{"begin":765,"end":766},"obj":"Gene"},{"id":"714","span":{"begin":752,"end":753},"obj":"Gene"},{"id":"715","span":{"begin":609,"end":610},"obj":"Gene"},{"id":"716","span":{"begin":550,"end":551},"obj":"Gene"},{"id":"717","span":{"begin":538,"end":539},"obj":"Gene"},{"id":"718","span":{"begin":406,"end":407},"obj":"Gene"},{"id":"719","span":{"begin":207,"end":222},"obj":"Species"},{"id":"720","span":{"begin":240,"end":245},"obj":"Species"},{"id":"721","span":{"begin":288,"end":291},"obj":"Species"},{"id":"722","span":{"begin":399,"end":405},"obj":"Species"},{"id":"723","span":{"begin":544,"end":549},"obj":"Species"},{"id":"724","span":{"begin":603,"end":608},"obj":"Species"},{"id":"725","span":{"begin":758,"end":764},"obj":"Species"},{"id":"726","span":{"begin":493,"end":511},"obj":"Disease"},{"id":"727","span":{"begin":571,"end":577},"obj":"CellLine"},{"id":"729","span":{"begin":836,"end":841},"obj":"Species"},{"id":"739","span":{"begin":1134,"end":1138},"obj":"Gene"},{"id":"740","span":{"begin":1268,"end":1272},"obj":"Gene"},{"id":"741","span":{"begin":1221,"end":1222},"obj":"Gene"},{"id":"742","span":{"begin":1020,"end":1021},"obj":"Gene"},{"id":"743","span":{"begin":1007,"end":1008},"obj":"Gene"},{"id":"744","span":{"begin":969,"end":970},"obj":"Gene"},{"id":"745","span":{"begin":947,"end":948},"obj":"Gene"},{"id":"746","span":{"begin":962,"end":968},"obj":"Species"},{"id":"747","span":{"begin":1013,"end":1019},"obj":"Species"}],"attributes":[{"id":"A696","pred":"tao:has_database_id","subj":"696","obj":"Tax:2697049"},{"id":"A697","pred":"tao:has_database_id","subj":"697","obj":"MESH:D007239"},{"id":"A713","pred":"tao:has_database_id","subj":"713","obj":"Gene:43740568"},{"id":"A714","pred":"tao:has_database_id","subj":"714","obj":"Gene:43740568"},{"id":"A715","pred":"tao:has_database_id","subj":"715","obj":"Gene:43740568"},{"id":"A716","pred":"tao:has_database_id","subj":"716","obj":"Gene:43740568"},{"id":"A717","pred":"tao:has_database_id","subj":"717","obj":"Gene:43740568"},{"id":"A718","pred":"tao:has_database_id","subj":"718","obj":"Gene:43740568"},{"id":"A719","pred":"tao:has_database_id","subj":"719","obj":"Tax:10090"},{"id":"A720","pred":"tao:has_database_id","subj":"720","obj":"Tax:9606"},{"id":"A721","pred":"tao:has_database_id","subj":"721","obj":"Tax:10116"},{"id":"A722","pred":"tao:has_database_id","subj":"722","obj":"Tax:2697049"},{"id":"A723","pred":"tao:has_database_id","subj":"723","obj":"Tax:2697049"},{"id":"A724","pred":"tao:has_database_id","subj":"724","obj":"Tax:2697049"},{"id":"A725","pred":"tao:has_database_id","subj":"725","obj":"Tax:2697049"},{"id":"A726","pred":"tao:has_database_id","subj":"726","obj":"MESH:D002303"},{"id":"A727","pred":"tao:has_database_id","subj":"727","obj":"CVCL:0574"},{"id":"A729","pred":"tao:has_database_id","subj":"729","obj":"Tax:9606"},{"id":"A739","pred":"tao:has_database_id","subj":"739","obj":"Gene:59272"},{"id":"A740","pred":"tao:has_database_id","subj":"740","obj":"Gene:59272"},{"id":"A741","pred":"tao:has_database_id","subj":"741","obj":"Gene:43740568"},{"id":"A742","pred":"tao:has_database_id","subj":"742","obj":"Gene:43740568"},{"id":"A743","pred":"tao:has_database_id","subj":"743","obj":"Gene:43740568"},{"id":"A744","pred":"tao:has_database_id","subj":"744","obj":"Gene:43740568"},{"id":"A745","pred":"tao:has_database_id","subj":"745","obj":"Gene:43740568"},{"id":"A746","pred":"tao:has_database_id","subj":"746","obj":"Tax:2697049"},{"id":"A747","pred":"tao:has_database_id","subj":"747","obj":"Tax:2697049"}],"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":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T150","span":{"begin":21,"end":28},"obj":"Body_part"},{"id":"T151","span":{"begin":171,"end":179},"obj":"Body_part"},{"id":"T152","span":{"begin":246,"end":260},"obj":"Body_part"},{"id":"T153","span":{"begin":299,"end":313},"obj":"Body_part"},{"id":"T154","span":{"begin":438,"end":446},"obj":"Body_part"},{"id":"T155","span":{"begin":578,"end":583},"obj":"Body_part"},{"id":"T156","span":{"begin":842,"end":846},"obj":"Body_part"},{"id":"T157","span":{"begin":847,"end":852},"obj":"Body_part"},{"id":"T158","span":{"begin":1048,"end":1056},"obj":"Body_part"}],"attributes":[{"id":"A150","pred":"fma_id","subj":"T150","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A151","pred":"fma_id","subj":"T151","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A152","pred":"fma_id","subj":"T152","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A153","pred":"fma_id","subj":"T153","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A154","pred":"fma_id","subj":"T154","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A155","pred":"fma_id","subj":"T155","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A156","pred":"fma_id","subj":"T156","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A157","pred":"fma_id","subj":"T157","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A158","pred":"fma_id","subj":"T158","obj":"http://purl.org/sig/ont/fma/fma62871"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T21","span":{"begin":842,"end":846},"obj":"Body_part"}],"attributes":[{"id":"A21","pred":"uberon_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T151","span":{"begin":107,"end":111},"obj":"Disease"},{"id":"T152","span":{"begin":117,"end":126},"obj":"Disease"},{"id":"T153","span":{"begin":388,"end":392},"obj":"Disease"},{"id":"T154","span":{"begin":399,"end":403},"obj":"Disease"},{"id":"T155","span":{"begin":533,"end":537},"obj":"Disease"},{"id":"T156","span":{"begin":592,"end":596},"obj":"Disease"},{"id":"T157","span":{"begin":747,"end":751},"obj":"Disease"},{"id":"T158","span":{"begin":758,"end":762},"obj":"Disease"},{"id":"T159","span":{"begin":942,"end":946},"obj":"Disease"},{"id":"T160","span":{"begin":962,"end":966},"obj":"Disease"},{"id":"T161","span":{"begin":1002,"end":1006},"obj":"Disease"},{"id":"T162","span":{"begin":1013,"end":1017},"obj":"Disease"},{"id":"T163","span":{"begin":1216,"end":1220},"obj":"Disease"}],"attributes":[{"id":"A151","pred":"mondo_id","subj":"T151","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A152","pred":"mondo_id","subj":"T152","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A153","pred":"mondo_id","subj":"T153","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A154","pred":"mondo_id","subj":"T154","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A155","pred":"mondo_id","subj":"T155","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A156","pred":"mondo_id","subj":"T156","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A157","pred":"mondo_id","subj":"T157","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A158","pred":"mondo_id","subj":"T158","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A159","pred":"mondo_id","subj":"T159","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A160","pred":"mondo_id","subj":"T160","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A161","pred":"mondo_id","subj":"T161","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A162","pred":"mondo_id","subj":"T162","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A163","pred":"mondo_id","subj":"T163","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T240","span":{"begin":49,"end":50},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T241","span":{"begin":89,"end":94},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T242","span":{"begin":137,"end":146},"obj":"http://purl.obolibrary.org/obo/CLO_0036932"},{"id":"T243","span":{"begin":240,"end":245},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T244","span":{"begin":462,"end":463},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T245","span":{"begin":483,"end":491},"obj":"http://purl.obolibrary.org/obo/CLO_0001658"},{"id":"T246","span":{"begin":571,"end":583},"obj":"http://purl.obolibrary.org/obo/CLO_0051719"},{"id":"T247","span":{"begin":623,"end":628},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T248","span":{"begin":716,"end":718},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T249","span":{"begin":836,"end":841},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T250","span":{"begin":842,"end":846},"obj":"http://purl.obolibrary.org/obo/UBERON_0002048"},{"id":"T251","span":{"begin":842,"end":846},"obj":"http://www.ebi.ac.uk/efo/EFO_0000934"},{"id":"T252","span":{"begin":847,"end":870},"obj":"http://purl.obolibrary.org/obo/CL_0001034"},{"id":"T253","span":{"begin":885,"end":886},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T254","span":{"begin":928,"end":930},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T255","span":{"begin":928,"end":930},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T256","span":{"begin":1128,"end":1130},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T257","span":{"begin":1128,"end":1130},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T258","span":{"begin":1250,"end":1252},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T259","span":{"begin":1250,"end":1252},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T167","span":{"begin":21,"end":28},"obj":"Chemical"},{"id":"T168","span":{"begin":928,"end":930},"obj":"Chemical"},{"id":"T169","span":{"begin":1128,"end":1130},"obj":"Chemical"},{"id":"T170","span":{"begin":1250,"end":1252},"obj":"Chemical"}],"attributes":[{"id":"A167","pred":"chebi_id","subj":"T167","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A168","pred":"chebi_id","subj":"T168","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A169","pred":"chebi_id","subj":"T169","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A170","pred":"chebi_id","subj":"T170","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T19","span":{"begin":246,"end":260},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T20","span":{"begin":299,"end":313},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"},{"id":"T21","span":{"begin":1167,"end":1190},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A19","pred":"meddra_id","subj":"T19","obj":"http://purl.bioontology.org/ontology/MEDDRA/10021496"},{"id":"A20","pred":"meddra_id","subj":"T20","obj":"http://purl.bioontology.org/ontology/MEDDRA/10021496"},{"id":"A21","pred":"meddra_id","subj":"T21","obj":"http://purl.bioontology.org/ontology/MEDDRA/10058063"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T95","span":{"begin":89,"end":94},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T96","span":{"begin":117,"end":126},"obj":"http://purl.obolibrary.org/obo/IDO_0000586"},{"id":"T97","span":{"begin":578,"end":583},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T98","span":{"begin":623,"end":628},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T99","span":{"begin":847,"end":852},"obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T109","span":{"begin":21,"end":28},"obj":"Chemical"}],"attributes":[{"id":"A109","pred":"chebi_id","subj":"T109","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T196","span":{"begin":107,"end":116},"obj":"Species"},{"id":"T197","span":{"begin":218,"end":222},"obj":"Species"},{"id":"T199","span":{"begin":240,"end":245},"obj":"Species"},{"id":"T200","span":{"begin":288,"end":291},"obj":"Species"},{"id":"T202","span":{"begin":388,"end":392},"obj":"Species"},{"id":"T203","span":{"begin":399,"end":405},"obj":"Species"},{"id":"T204","span":{"begin":533,"end":537},"obj":"Species"},{"id":"T205","span":{"begin":544,"end":549},"obj":"Species"},{"id":"T206","span":{"begin":592,"end":596},"obj":"Species"},{"id":"T207","span":{"begin":603,"end":608},"obj":"Species"},{"id":"T208","span":{"begin":747,"end":751},"obj":"Species"},{"id":"T209","span":{"begin":758,"end":764},"obj":"Species"},{"id":"T210","span":{"begin":836,"end":841},"obj":"Species"},{"id":"T211","span":{"begin":942,"end":946},"obj":"Species"},{"id":"T212","span":{"begin":962,"end":968},"obj":"Species"},{"id":"T213","span":{"begin":1002,"end":1006},"obj":"Species"},{"id":"T214","span":{"begin":1013,"end":1019},"obj":"Species"},{"id":"T215","span":{"begin":1216,"end":1220},"obj":"Species"}],"attributes":[{"id":"A200","pred":"ncbi_taxonomy_id","subj":"T200","obj":"NCBItxid:10116"},{"id":"A201","pred":"ncbi_taxonomy_id","subj":"T200","obj":"NCBItxid:10114"},{"id":"A213","pred":"ncbi_taxonomy_id","subj":"T213","obj":"NCBItxid:694009"},{"id":"A210","pred":"ncbi_taxonomy_id","subj":"T210","obj":"NCBItxid:9606"},{"id":"A202","pred":"ncbi_taxonomy_id","subj":"T202","obj":"NCBItxid:694009"},{"id":"A212","pred":"ncbi_taxonomy_id","subj":"T212","obj":"NCBItxid:2697049"},{"id":"A196","pred":"ncbi_taxonomy_id","subj":"T196","obj":"NCBItxid:2697049"},{"id":"A207","pred":"ncbi_taxonomy_id","subj":"T207","obj":"NCBItxid:2697049"},{"id":"A206","pred":"ncbi_taxonomy_id","subj":"T206","obj":"NCBItxid:694009"},{"id":"A204","pred":"ncbi_taxonomy_id","subj":"T204","obj":"NCBItxid:694009"},{"id":"A211","pred":"ncbi_taxonomy_id","subj":"T211","obj":"NCBItxid:694009"},{"id":"A215","pred":"ncbi_taxonomy_id","subj":"T215","obj":"NCBItxid:694009"},{"id":"A214","pred":"ncbi_taxonomy_id","subj":"T214","obj":"NCBItxid:2697049"},{"id":"A199","pred":"ncbi_taxonomy_id","subj":"T199","obj":"NCBItxid:9606"},{"id":"A208","pred":"ncbi_taxonomy_id","subj":"T208","obj":"NCBItxid:694009"},{"id":"A203","pred":"ncbi_taxonomy_id","subj":"T203","obj":"NCBItxid:2697049"},{"id":"A205","pred":"ncbi_taxonomy_id","subj":"T205","obj":"NCBItxid:2697049"},{"id":"A197","pred":"ncbi_taxonomy_id","subj":"T197","obj":"NCBItxid:10095"},{"id":"A198","pred":"ncbi_taxonomy_id","subj":"T197","obj":"NCBItxid:10088"},{"id":"A209","pred":"ncbi_taxonomy_id","subj":"T209","obj":"NCBItxid:2697049"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T165","span":{"begin":0,"end":28},"obj":"Sentence"},{"id":"T166","span":{"begin":30,"end":48},"obj":"Sentence"},{"id":"T167","span":{"begin":49,"end":126},"obj":"Sentence"},{"id":"T168","span":{"begin":127,"end":413},"obj":"Sentence"},{"id":"T169","span":{"begin":414,"end":634},"obj":"Sentence"},{"id":"T170","span":{"begin":635,"end":767},"obj":"Sentence"},{"id":"T171","span":{"begin":769,"end":785},"obj":"Sentence"},{"id":"T172","span":{"begin":786,"end":870},"obj":"Sentence"},{"id":"T173","span":{"begin":871,"end":971},"obj":"Sentence"},{"id":"T174","span":{"begin":972,"end":1153},"obj":"Sentence"},{"id":"T175","span":{"begin":1154,"end":1273},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-UBERON","denotations":[{"id":"T21","span":{"begin":842,"end":846},"obj":"Body_part"}],"attributes":[{"id":"A21","pred":"uberon_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"696","span":{"begin":107,"end":116},"obj":"Species"},{"id":"697","span":{"begin":117,"end":126},"obj":"Disease"},{"id":"719","span":{"begin":207,"end":222},"obj":"Species"},{"id":"720","span":{"begin":240,"end":245},"obj":"Species"},{"id":"721","span":{"begin":288,"end":291},"obj":"Species"},{"id":"722","span":{"begin":399,"end":405},"obj":"Species"},{"id":"718","span":{"begin":406,"end":407},"obj":"Gene"},{"id":"726","span":{"begin":493,"end":511},"obj":"Disease"},{"id":"717","span":{"begin":538,"end":539},"obj":"Gene"},{"id":"723","span":{"begin":544,"end":549},"obj":"Species"},{"id":"716","span":{"begin":550,"end":551},"obj":"Gene"},{"id":"727","span":{"begin":571,"end":577},"obj":"CellLine"},{"id":"724","span":{"begin":603,"end":608},"obj":"Species"},{"id":"715","span":{"begin":609,"end":610},"obj":"Gene"},{"id":"714","span":{"begin":752,"end":753},"obj":"Gene"},{"id":"725","span":{"begin":758,"end":764},"obj":"Species"},{"id":"713","span":{"begin":765,"end":766},"obj":"Gene"},{"id":"729","span":{"begin":836,"end":841},"obj":"Species"},{"id":"745","span":{"begin":947,"end":948},"obj":"Gene"},{"id":"746","span":{"begin":962,"end":968},"obj":"Species"},{"id":"744","span":{"begin":969,"end":970},"obj":"Gene"},{"id":"743","span":{"begin":1007,"end":1008},"obj":"Gene"},{"id":"747","span":{"begin":1013,"end":1019},"obj":"Species"},{"id":"742","span":{"begin":1020,"end":1021},"obj":"Gene"},{"id":"739","span":{"begin":1134,"end":1138},"obj":"Gene"},{"id":"741","span":{"begin":1221,"end":1222},"obj":"Gene"},{"id":"740","span":{"begin":1268,"end":1272},"obj":"Gene"}],"attributes":[{"id":"A724","pred":"pubann:denotes","subj":"724","obj":"Tax:2697049"},{"id":"A721","pred":"pubann:denotes","subj":"721","obj":"Tax:10116"},{"id":"A743","pred":"pubann:denotes","subj":"743","obj":"Gene:43740568"},{"id":"A742","pred":"pubann:denotes","subj":"742","obj":"Gene:43740568"},{"id":"A714","pred":"pubann:denotes","subj":"714","obj":"Gene:43740568"},{"id":"A715","pred":"pubann:denotes","subj":"715","obj":"Gene:43740568"},{"id":"A720","pred":"pubann:denotes","subj":"720","obj":"Tax:9606"},{"id":"A723","pred":"pubann:denotes","subj":"723","obj":"Tax:2697049"},{"id":"A740","pred":"pubann:denotes","subj":"740","obj":"Gene:59272"},{"id":"A696","pred":"pubann:denotes","subj":"696","obj":"Tax:2697049"},{"id":"A746","pred":"pubann:denotes","subj":"746","obj":"Tax:2697049"},{"id":"A725","pred":"pubann:denotes","subj":"725","obj":"Tax:2697049"},{"id":"A718","pred":"pubann:denotes","subj":"718","obj":"Gene:43740568"},{"id":"A697","pred":"pubann:denotes","subj":"697","obj":"MESH:D007239"},{"id":"A739","pred":"pubann:denotes","subj":"739","obj":"Gene:59272"},{"id":"A744","pred":"pubann:denotes","subj":"744","obj":"Gene:43740568"},{"id":"A747","pred":"pubann:denotes","subj":"747","obj":"Tax:2697049"},{"id":"A726","pred":"pubann:denotes","subj":"726","obj":"MESH:D002303"},{"id":"A716","pred":"pubann:denotes","subj":"716","obj":"Gene:43740568"},{"id":"A741","pred":"pubann:denotes","subj":"741","obj":"Gene:43740568"},{"id":"A713","pred":"pubann:denotes","subj":"713","obj":"Gene:43740568"},{"id":"A745","pred":"pubann:denotes","subj":"745","obj":"Gene:43740568"},{"id":"A727","pred":"pubann:denotes","subj":"727","obj":"CVCL:0574"},{"id":"A722","pred":"pubann:denotes","subj":"722","obj":"Tax:2697049"},{"id":"A729","pred":"pubann:denotes","subj":"729","obj":"Tax:9606"},{"id":"A719","pred":"pubann:denotes","subj":"719","obj":"Tax:10090"},{"id":"A717","pred":"pubann:denotes","subj":"717","obj":"Gene:43740568"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

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Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-MAT","denotations":[{"id":"T5","span":{"begin":842,"end":846},"obj":"http://purl.obolibrary.org/obo/MAT_0000135"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T30","span":{"begin":512,"end":521},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T150","span":{"begin":21,"end":28},"obj":"Body_part"},{"id":"T151","span":{"begin":171,"end":179},"obj":"Body_part"},{"id":"T152","span":{"begin":246,"end":260},"obj":"Body_part"},{"id":"T153","span":{"begin":299,"end":313},"obj":"Body_part"},{"id":"T154","span":{"begin":438,"end":446},"obj":"Body_part"},{"id":"T155","span":{"begin":578,"end":583},"obj":"Body_part"},{"id":"T156","span":{"begin":842,"end":846},"obj":"Body_part"},{"id":"T157","span":{"begin":847,"end":852},"obj":"Body_part"},{"id":"T158","span":{"begin":1048,"end":1056},"obj":"Body_part"}],"attributes":[{"id":"A156","pred":"fma_id","subj":"T156","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A151","pred":"fma_id","subj":"T151","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A153","pred":"fma_id","subj":"T153","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A155","pred":"fma_id","subj":"T155","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A150","pred":"fma_id","subj":"T150","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A154","pred":"fma_id","subj":"T154","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A158","pred":"fma_id","subj":"T158","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A152","pred":"fma_id","subj":"T152","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A157","pred":"fma_id","subj":"T157","obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T146","span":{"begin":107,"end":116},"obj":"Disease"},{"id":"T147","span":{"begin":117,"end":126},"obj":"Disease"},{"id":"T148","span":{"begin":388,"end":392},"obj":"Disease"},{"id":"T149","span":{"begin":399,"end":403},"obj":"Disease"},{"id":"T150","span":{"begin":533,"end":537},"obj":"Disease"},{"id":"T151","span":{"begin":592,"end":596},"obj":"Disease"},{"id":"T152","span":{"begin":747,"end":751},"obj":"Disease"},{"id":"T153","span":{"begin":758,"end":762},"obj":"Disease"},{"id":"T154","span":{"begin":942,"end":946},"obj":"Disease"},{"id":"T155","span":{"begin":962,"end":966},"obj":"Disease"},{"id":"T156","span":{"begin":1002,"end":1006},"obj":"Disease"},{"id":"T157","span":{"begin":1013,"end":1017},"obj":"Disease"},{"id":"T158","span":{"begin":1216,"end":1220},"obj":"Disease"}],"attributes":[{"id":"A151","pred":"mondo_id","subj":"T151","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A147","pred":"mondo_id","subj":"T147","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A157","pred":"mondo_id","subj":"T157","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A156","pred":"mondo_id","subj":"T156","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A150","pred":"mondo_id","subj":"T150","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A149","pred":"mondo_id","subj":"T149","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A148","pred":"mondo_id","subj":"T148","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A152","pred":"mondo_id","subj":"T152","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A155","pred":"mondo_id","subj":"T155","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A154","pred":"mondo_id","subj":"T154","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A146","pred":"mondo_id","subj":"T146","obj":"http://purl.obolibrary.org/obo/MONDO_0100096"},{"id":"A153","pred":"mondo_id","subj":"T153","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A158","pred":"mondo_id","subj":"T158","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T26","span":{"begin":512,"end":521},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T26","span":{"begin":512,"end":521},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}

{"project":"LitCovid-sentences","denotations":[{"id":"T165","span":{"begin":0,"end":28},"obj":"Sentence"},{"id":"T166","span":{"begin":30,"end":48},"obj":"Sentence"},{"id":"T167","span":{"begin":49,"end":126},"obj":"Sentence"},{"id":"T168","span":{"begin":127,"end":413},"obj":"Sentence"},{"id":"T169","span":{"begin":414,"end":634},"obj":"Sentence"},{"id":"T170","span":{"begin":635,"end":767},"obj":"Sentence"},{"id":"T171","span":{"begin":769,"end":785},"obj":"Sentence"},{"id":"T172","span":{"begin":786,"end":870},"obj":"Sentence"},{"id":"T173","span":{"begin":871,"end":971},"obj":"Sentence"},{"id":"T174","span":{"begin":972,"end":1153},"obj":"Sentence"},{"id":"T175","span":{"begin":1154,"end":1273},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"6.1 Targeting the S protein\n\n6.1.1 Hypothesis: A mAb against the binding domain of the virus can inhibit SARS-CoV2 infection\nRecently, hybridoma supernatants containing antibody repertoires from immunized transgenic mice that express the human immunoglobulin heavy and light chains and rat origin immunoglobulin constant regions were used to detect antibodies that can cross neutralize SARS-S and SARS-2-S [26]. One chimeric 47D11 H2L2 antibody displayed such a cross-neutralizing activity, decreased syncytia formation induced by SARS-S and SARS2-S, and could protect VeroE6 cells against SARS-S and SARS2-S pseudotyped virus [26]. It may lie in its similar affinities for interacting with the same domain of the S1 subunit, i.e., S1B, of each SARS-S and SARS-2-S.\n\n6.1.2 Rational: The chimeric 47D11 H2L2 might not be effective in human lung cells as it is in vitro\n47D11 carried a higher affinity for interacting with the S2 subunit of SARS-S than that of SARS-2-S. It is important that for both SARS-S and SARS-2-S, the binding of the 47D11 antibody to the target – the S1B domain – does not block the binding of S1B and S2 to ACE2 receptor [26]. By contrast, neutralizing antibodies that specifically target SARS-S could compete with S1B and S2 for binding to ACE2."}