PMC:7376845 / 120-1817 JSON TXT

Annnotations TAB JSON ListView MergeView

LitCovid-PD-FMA-UBERON

LitCovid-PubTator

LitCovid-PD-MONDO

LitCovid-PD-CLO

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T3","span":{"begin":11,"end":12},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T4","span":{"begin":98,"end":101},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T5","span":{"begin":124,"end":129},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T6","span":{"begin":314,"end":318},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":509,"end":512},"obj":"http://purl.obolibrary.org/obo/PR_000001343"},{"id":"T8","span":{"begin":901,"end":907},"obj":"http://purl.obolibrary.org/obo/UBERON_0000473"},{"id":"T9","span":{"begin":933,"end":938},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T10","span":{"begin":950,"end":955},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T11","span":{"begin":1001,"end":1002},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T12","span":{"begin":1019,"end":1021},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T13","span":{"begin":1019,"end":1021},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T14","span":{"begin":1160,"end":1162},"obj":"http://purl.obolibrary.org/obo/CLO_0008922"},{"id":"T15","span":{"begin":1160,"end":1162},"obj":"http://purl.obolibrary.org/obo/CLO_0050052"},{"id":"T16","span":{"begin":1249,"end":1254},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9606"},{"id":"T17","span":{"begin":1400,"end":1410},"obj":"http://purl.obolibrary.org/obo/CLO_0000031"},{"id":"T18","span":{"begin":1495,"end":1500},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T19","span":{"begin":1528,"end":1529},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Background\nA novel coronavirus, SARS-CoV-2, which emerged at the end of 2019 and causes COVID-19, has resulted in worldwide human infections. While genetically distinct, SARS-CoV-1, the aetiological agent responsible for an outbreak of severe acute respiratory syndrome (SARS) in 2002–2003, utilises the same host cell receptor as SARS-CoV-2 for entry: angiotensin-converting enzyme 2 (ACE2). Parts of the SARS-CoV-1 spike glycoprotein (S protein), which interacts with ACE2, appear conserved in SARS-CoV-2.\n\nAim\nThe cross-reactivity with SARS-CoV-2 of monoclonal antibodies (mAbs) previously generated against the S protein of SARS-CoV-1 was assessed.\n\nMethods\nThe SARS-CoV-2 S protein sequence was aligned to those of SARS-CoV-1, Middle East respiratory syndrome (MERS) and common-cold coronaviruses. Abilities of mAbs generated against SARS-CoV-1 S protein to bind SARS-CoV-2 or its S protein were tested with SARS-CoV-2 infected cells as well as cells expressing either the full length protein or a fragment of its S2 subunit. Quantitative ELISA was also performed to compare binding of mAbs to recombinant S protein.\n\nResults\nAn immunogenic domain in the S2 subunit of SARS-CoV-1 S protein is highly conserved in SARS-CoV-2 but not in MERS and human common-cold coronaviruses. Four murine mAbs raised against this immunogenic fragment could recognise SARS-CoV-2 S protein expressed in mammalian cell lines. In particular, mAb 1A9 was demonstrated to detect S protein in SARS-CoV-2-infected cells and is suitable for use in a sandwich ELISA format.\n\nConclusion\nThe cross-reactive mAbs may serve as useful tools for SARS-CoV-2 research and for the development of diagnostic assays for COVID-19."}

LitCovid-PD-CHEBI

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T2","span":{"begin":353,"end":364},"obj":"Chemical"},{"id":"T3","span":{"begin":423,"end":435},"obj":"Chemical"},{"id":"T4","span":{"begin":439,"end":446},"obj":"Chemical"},{"id":"T5","span":{"begin":617,"end":624},"obj":"Chemical"},{"id":"T6","span":{"begin":679,"end":686},"obj":"Chemical"},{"id":"T7","span":{"begin":852,"end":859},"obj":"Chemical"},{"id":"T8","span":{"begin":888,"end":895},"obj":"Chemical"},{"id":"T9","span":{"begin":990,"end":997},"obj":"Chemical"},{"id":"T10","span":{"begin":1019,"end":1021},"obj":"Chemical"},{"id":"T11","span":{"begin":1113,"end":1120},"obj":"Chemical"},{"id":"T12","span":{"begin":1160,"end":1162},"obj":"Chemical"},{"id":"T13","span":{"begin":1187,"end":1194},"obj":"Chemical"},{"id":"T14","span":{"begin":1369,"end":1376},"obj":"Chemical"},{"id":"T15","span":{"begin":1464,"end":1471},"obj":"Chemical"}],"attributes":[{"id":"A2","pred":"chebi_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CHEBI_48433"},{"id":"A3","pred":"chebi_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A4","pred":"chebi_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A5","pred":"chebi_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A6","pred":"chebi_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A7","pred":"chebi_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A8","pred":"chebi_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A9","pred":"chebi_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A10","pred":"chebi_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A11","pred":"chebi_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A12","pred":"chebi_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/CHEBI_29387"},{"id":"A13","pred":"chebi_id","subj":"T13","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A14","pred":"chebi_id","subj":"T14","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A15","pred":"chebi_id","subj":"T15","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Background\nA novel coronavirus, SARS-CoV-2, which emerged at the end of 2019 and causes COVID-19, has resulted in worldwide human infections. While genetically distinct, SARS-CoV-1, the aetiological agent responsible for an outbreak of severe acute respiratory syndrome (SARS) in 2002–2003, utilises the same host cell receptor as SARS-CoV-2 for entry: angiotensin-converting enzyme 2 (ACE2). Parts of the SARS-CoV-1 spike glycoprotein (S protein), which interacts with ACE2, appear conserved in SARS-CoV-2.\n\nAim\nThe cross-reactivity with SARS-CoV-2 of monoclonal antibodies (mAbs) previously generated against the S protein of SARS-CoV-1 was assessed.\n\nMethods\nThe SARS-CoV-2 S protein sequence was aligned to those of SARS-CoV-1, Middle East respiratory syndrome (MERS) and common-cold coronaviruses. Abilities of mAbs generated against SARS-CoV-1 S protein to bind SARS-CoV-2 or its S protein were tested with SARS-CoV-2 infected cells as well as cells expressing either the full length protein or a fragment of its S2 subunit. Quantitative ELISA was also performed to compare binding of mAbs to recombinant S protein.\n\nResults\nAn immunogenic domain in the S2 subunit of SARS-CoV-1 S protein is highly conserved in SARS-CoV-2 but not in MERS and human common-cold coronaviruses. Four murine mAbs raised against this immunogenic fragment could recognise SARS-CoV-2 S protein expressed in mammalian cell lines. In particular, mAb 1A9 was demonstrated to detect S protein in SARS-CoV-2-infected cells and is suitable for use in a sandwich ELISA format.\n\nConclusion\nThe cross-reactive mAbs may serve as useful tools for SARS-CoV-2 research and for the development of diagnostic assays for COVID-19."}

LitCovid-sentences

{"project":"LitCovid-sentences","denotations":[{"id":"T3","span":{"begin":0,"end":10},"obj":"Sentence"},{"id":"T4","span":{"begin":11,"end":141},"obj":"Sentence"},{"id":"T5","span":{"begin":142,"end":392},"obj":"Sentence"},{"id":"T6","span":{"begin":393,"end":507},"obj":"Sentence"},{"id":"T7","span":{"begin":509,"end":512},"obj":"Sentence"},{"id":"T8","span":{"begin":513,"end":652},"obj":"Sentence"},{"id":"T9","span":{"begin":654,"end":661},"obj":"Sentence"},{"id":"T10","span":{"begin":662,"end":802},"obj":"Sentence"},{"id":"T11","span":{"begin":803,"end":1030},"obj":"Sentence"},{"id":"T12","span":{"begin":1031,"end":1121},"obj":"Sentence"},{"id":"T13","span":{"begin":1123,"end":1130},"obj":"Sentence"},{"id":"T14","span":{"begin":1131,"end":1281},"obj":"Sentence"},{"id":"T15","span":{"begin":1282,"end":1411},"obj":"Sentence"},{"id":"T16","span":{"begin":1412,"end":1552},"obj":"Sentence"},{"id":"T17","span":{"begin":1554,"end":1564},"obj":"Sentence"},{"id":"T18","span":{"begin":1565,"end":1697},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Background\nA novel coronavirus, SARS-CoV-2, which emerged at the end of 2019 and causes COVID-19, has resulted in worldwide human infections. While genetically distinct, SARS-CoV-1, the aetiological agent responsible for an outbreak of severe acute respiratory syndrome (SARS) in 2002–2003, utilises the same host cell receptor as SARS-CoV-2 for entry: angiotensin-converting enzyme 2 (ACE2). Parts of the SARS-CoV-1 spike glycoprotein (S protein), which interacts with ACE2, appear conserved in SARS-CoV-2.\n\nAim\nThe cross-reactivity with SARS-CoV-2 of monoclonal antibodies (mAbs) previously generated against the S protein of SARS-CoV-1 was assessed.\n\nMethods\nThe SARS-CoV-2 S protein sequence was aligned to those of SARS-CoV-1, Middle East respiratory syndrome (MERS) and common-cold coronaviruses. Abilities of mAbs generated against SARS-CoV-1 S protein to bind SARS-CoV-2 or its S protein were tested with SARS-CoV-2 infected cells as well as cells expressing either the full length protein or a fragment of its S2 subunit. Quantitative ELISA was also performed to compare binding of mAbs to recombinant S protein.\n\nResults\nAn immunogenic domain in the S2 subunit of SARS-CoV-1 S protein is highly conserved in SARS-CoV-2 but not in MERS and human common-cold coronaviruses. Four murine mAbs raised against this immunogenic fragment could recognise SARS-CoV-2 S protein expressed in mammalian cell lines. In particular, mAb 1A9 was demonstrated to detect S protein in SARS-CoV-2-infected cells and is suitable for use in a sandwich ELISA format.\n\nConclusion\nThe cross-reactive mAbs may serve as useful tools for SARS-CoV-2 research and for the development of diagnostic assays for COVID-19."}