PMC:7048180 / 5943-7570 JSONTXT

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T21","span":{"begin":61,"end":68},"obj":"Body_part"},{"id":"T22","span":{"begin":520,"end":525},"obj":"Body_part"},{"id":"T23","span":{"begin":625,"end":633},"obj":"Body_part"},{"id":"T24","span":{"begin":844,"end":850},"obj":"Body_part"},{"id":"T25","span":{"begin":890,"end":896},"obj":"Body_part"},{"id":"T26","span":{"begin":1049,"end":1056},"obj":"Body_part"},{"id":"T27","span":{"begin":1436,"end":1443},"obj":"Body_part"},{"id":"T28","span":{"begin":1601,"end":1608},"obj":"Body_part"}],"attributes":[{"id":"A21","pred":"fma_id","subj":"T21","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A22","pred":"fma_id","subj":"T22","obj":"http://purl.org/sig/ont/fma/fma60992"},{"id":"A23","pred":"fma_id","subj":"T23","obj":"http://purl.org/sig/ont/fma/fma82763"},{"id":"A24","pred":"fma_id","subj":"T24","obj":"http://purl.org/sig/ont/fma/fma82758"},{"id":"A25","pred":"fma_id","subj":"T25","obj":"http://purl.org/sig/ont/fma/fma82766"},{"id":"A26","pred":"fma_id","subj":"T26","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A27","pred":"fma_id","subj":"T27","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A28","pred":"fma_id","subj":"T28","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T1","span":{"begin":520,"end":525},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002488"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

{"project":"LitCovid_AGAC","denotations":[{"id":"p8111s23","span":{"begin":704,"end":713},"obj":"NegReg"},{"id":"p8111s25","span":{"begin":718,"end":724},"obj":"MPA"},{"id":"p8111s26","span":{"begin":725,"end":743},"obj":"MPA"},{"id":"p8111s33","span":{"begin":764,"end":772},"obj":"NegReg"},{"id":"p8111s36","span":{"begin":780,"end":804},"obj":"Interaction"},{"id":"p8112s39","span":{"begin":994,"end":1009},"obj":"MPA"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T37","span":{"begin":246,"end":254},"obj":"Disease"},{"id":"T38","span":{"begin":529,"end":537},"obj":"Disease"},{"id":"T39","span":{"begin":643,"end":651},"obj":"Disease"},{"id":"T40","span":{"begin":906,"end":914},"obj":"Disease"},{"id":"T41","span":{"begin":1114,"end":1122},"obj":"Disease"},{"id":"T42","span":{"begin":1421,"end":1429},"obj":"Disease"}],"attributes":[{"id":"A37","pred":"mondo_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A38","pred":"mondo_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A39","pred":"mondo_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A40","pred":"mondo_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A41","pred":"mondo_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A42","pred":"mondo_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T38","span":{"begin":167,"end":172},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T39","span":{"begin":549,"end":550},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T40","span":{"begin":577,"end":578},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T41","span":{"begin":762,"end":763},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T42","span":{"begin":842,"end":843},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T43","span":{"begin":1092,"end":1093},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T44","span":{"begin":1185,"end":1190},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T45","span":{"begin":1352,"end":1357},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T46","span":{"begin":1449,"end":1454},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

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{"project":"LitCovid-sentences","denotations":[{"id":"T35","span":{"begin":0,"end":69},"obj":"Sentence"},{"id":"T36","span":{"begin":70,"end":178},"obj":"Sentence"},{"id":"T37","span":{"begin":179,"end":352},"obj":"Sentence"},{"id":"T38","span":{"begin":353,"end":490},"obj":"Sentence"},{"id":"T39","span":{"begin":491,"end":611},"obj":"Sentence"},{"id":"T40","span":{"begin":612,"end":826},"obj":"Sentence"},{"id":"T41","span":{"begin":827,"end":1010},"obj":"Sentence"},{"id":"T42","span":{"begin":1011,"end":1132},"obj":"Sentence"},{"id":"T43","span":{"begin":1133,"end":1300},"obj":"Sentence"},{"id":"T44","span":{"begin":1301,"end":1473},"obj":"Sentence"},{"id":"T45","span":{"begin":1474,"end":1627},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}

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A266","pred":"tao:has_database_id","subj":"266","obj":"MESH:D006859"},{"id":"A268","pred":"tao:has_database_id","subj":"268","obj":"MESH:D006859"},{"id":"A270","pred":"tao:has_database_id","subj":"270","obj":"MESH:D001120"},{"id":"A271","pred":"tao:has_database_id","subj":"271","obj":"MESH:D001216"},{"id":"A272","pred":"tao:has_database_id","subj":"272","obj":"MESH:D008239"},{"id":"A274","pred":"tao:has_database_id","subj":"274","obj":"MESH:D014633"},{"id":"A275","pred":"tao:has_database_id","subj":"275","obj":"MESH:C005496"}],"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":"In this study, we first expressed and purified 2019-nCoV RBD protein. We also predicted the conformations of 2019-nCoV RBD and its complex with the putative receptor, human ACE2. Comparison of the interaction between the complex of ACE2 [13] and SARS-CoV RBD and homology model of ACE2 and 2019-nCoV RBD revealed similar binding modes (data not shown). In both complexes, β5–β6 loop and β6–β7 loop form extensive contact, including at least seven pairs of hydrogen bonds, with the receptor. Notably, R426 on the forth α helix in SARS-CoV RBD builds a salt bridge with E329 and a hydrogen bond with Q325 on ACE2. However, the arginine (R426 in SARS-CoV RBD) to asparagine (N439) mutation in 2019-nCoV RBD abolished the strong polar interactions, which may induce a decrease in the binding affinity between RBD and the receptor. Interestingly, a lysine (K417 in 2019-nCoV RBD) replacement of valine (V404 in SARS-CoV RBD) on β6 formed an extra salt bridge with D30 on ACE2, which may recover the binding ability. These data indicate that the RBD in S protein of 2019-nCoV may bind to ACE2 with a similar affinity as SARS-CoV RBD does. Indeed, we measured the binding of 2019-nCoV RBD to human ACE2 by the biolayer interferometry binding (BLI) assay, and found that 2019-nCoV RBD bound potently to ACE2. The calculated affinity (KD) of 2019-nCoV RBD with human ACE2 was 15.2 nM (Figure 1(f)), which is comparable to that of SARS-CoV spike protein with human ACE2 (15 nM) [14]. These results indicate that ACE2 could be the potential receptor for the new coronavirus, and that the expressed 2019-nCoV RBD protein is functional [2]."}