PMC:7352545 / 36742-37829 JSONTXT

{"project":"LitCovid_Glycan-Motif-Structure","denotations":[{"id":"T155","span":{"begin":149,"end":151},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T156","span":{"begin":690,"end":692},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T157","span":{"begin":715,"end":717},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T158","span":{"begin":845,"end":847},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T159","span":{"begin":1009,"end":1011},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T297","span":{"begin":91,"end":103},"obj":"Body_part"},{"id":"T298","span":{"begin":235,"end":242},"obj":"Body_part"},{"id":"T299","span":{"begin":287,"end":294},"obj":"Body_part"},{"id":"T300","span":{"begin":295,"end":301},"obj":"Body_part"},{"id":"T301","span":{"begin":601,"end":607},"obj":"Body_part"},{"id":"T302","span":{"begin":621,"end":637},"obj":"Body_part"},{"id":"T303","span":{"begin":632,"end":637},"obj":"Body_part"},{"id":"T304","span":{"begin":649,"end":656},"obj":"Body_part"},{"id":"T305","span":{"begin":668,"end":684},"obj":"Body_part"},{"id":"T306","span":{"begin":679,"end":684},"obj":"Body_part"},{"id":"T307","span":{"begin":780,"end":796},"obj":"Body_part"},{"id":"T308","span":{"begin":791,"end":796},"obj":"Body_part"},{"id":"T309","span":{"begin":801,"end":805},"obj":"Body_part"},{"id":"T310","span":{"begin":818,"end":834},"obj":"Body_part"},{"id":"T311","span":{"begin":829,"end":834},"obj":"Body_part"},{"id":"T312","span":{"begin":891,"end":898},"obj":"Body_part"},{"id":"T313","span":{"begin":926,"end":933},"obj":"Body_part"}],"attributes":[{"id":"A297","pred":"fma_id","subj":"T297","obj":"http://purl.org/sig/ont/fma/fma62845"},{"id":"A298","pred":"fma_id","subj":"T298","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A299","pred":"fma_id","subj":"T299","obj":"http://purl.org/sig/ont/fma/fma7394"},{"id":"A300","pred":"fma_id","subj":"T300","obj":"http://purl.org/sig/ont/fma/fma9637"},{"id":"A301","pred":"fma_id","subj":"T301","obj":"http://purl.org/sig/ont/fma/fma7203"},{"id":"A302","pred":"fma_id","subj":"T302","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A303","pred":"fma_id","subj":"T303","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A304","pred":"fma_id","subj":"T304","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A305","pred":"fma_id","subj":"T305","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A306","pred":"fma_id","subj":"T306","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A307","pred":"fma_id","subj":"T307","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A308","pred":"fma_id","subj":"T308","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A309","pred":"fma_id","subj":"T309","obj":"http://purl.org/sig/ont/fma/fma7195"},{"id":"A310","pred":"fma_id","subj":"T310","obj":"http://purl.org/sig/ont/fma/fma66768"},{"id":"A311","pred":"fma_id","subj":"T311","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A312","pred":"fma_id","subj":"T312","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A313","pred":"fma_id","subj":"T313","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-UBERON","denotations":[{"id":"T8","span":{"begin":287,"end":294},"obj":"Body_part"},{"id":"T9","span":{"begin":295,"end":301},"obj":"Body_part"},{"id":"T10","span":{"begin":601,"end":607},"obj":"Body_part"},{"id":"T11","span":{"begin":801,"end":805},"obj":"Body_part"}],"attributes":[{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0003126"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000479"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"A11","pred":"uberon_id","subj":"T11","obj":"http://purl.obolibrary.org/obo/UBERON_0002048"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T129","span":{"begin":53,"end":63},"obj":"Disease"},{"id":"T130","span":{"begin":191,"end":200},"obj":"Disease"},{"id":"T131","span":{"begin":758,"end":767},"obj":"Disease"}],"attributes":[{"id":"A129","pred":"mondo_id","subj":"T129","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A130","pred":"mondo_id","subj":"T130","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"},{"id":"A131","pred":"mondo_id","subj":"T131","obj":"http://purl.obolibrary.org/obo/MONDO_0005550"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T496","span":{"begin":91,"end":103},"obj":"http://purl.obolibrary.org/obo/CL_0000232"},{"id":"T497","span":{"begin":165,"end":166},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T498","span":{"begin":232,"end":234},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T499","span":{"begin":279,"end":286},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_9031"},{"id":"T500","span":{"begin":367,"end":372},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"},{"id":"T501","span":{"begin":417,"end":420},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T502","span":{"begin":528,"end":531},"obj":"http://purl.obolibrary.org/obo/CLO_0051582"},{"id":"T503","span":{"begin":601,"end":607},"obj":"http://purl.obolibrary.org/obo/UBERON_0002113"},{"id":"T504","span":{"begin":601,"end":607},"obj":"http://www.ebi.ac.uk/efo/EFO_0000927"},{"id":"T505","span":{"begin":601,"end":607},"obj":"http://www.ebi.ac.uk/efo/EFO_0000929"},{"id":"T506","span":{"begin":621,"end":631},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T507","span":{"begin":632,"end":637},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T508","span":{"begin":668,"end":678},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T509","span":{"begin":679,"end":684},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T510","span":{"begin":688,"end":689},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T511","span":{"begin":780,"end":805},"obj":"http://purl.obolibrary.org/obo/CL_0000082"},{"id":"T512","span":{"begin":818,"end":828},"obj":"http://purl.obolibrary.org/obo/CL_0000066"},{"id":"T513","span":{"begin":829,"end":834},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T514","span":{"begin":875,"end":877},"obj":"http://purl.obolibrary.org/obo/CLO_0050050"},{"id":"T515","span":{"begin":1066,"end":1073},"obj":"http://purl.obolibrary.org/obo/NCBITaxon_10239"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T1138","span":{"begin":135,"end":140},"obj":"Chemical"},{"id":"T1140","span":{"begin":149,"end":151},"obj":"Chemical"},{"id":"T1145","span":{"begin":235,"end":242},"obj":"Chemical"},{"id":"T1146","span":{"begin":552,"end":554},"obj":"Chemical"},{"id":"T1147","span":{"begin":649,"end":656},"obj":"Chemical"},{"id":"T1148","span":{"begin":690,"end":692},"obj":"Chemical"},{"id":"T1153","span":{"begin":715,"end":717},"obj":"Chemical"},{"id":"T1158","span":{"begin":845,"end":847},"obj":"Chemical"},{"id":"T1163","span":{"begin":891,"end":898},"obj":"Chemical"},{"id":"T1164","span":{"begin":926,"end":933},"obj":"Chemical"},{"id":"T1165","span":{"begin":1009,"end":1011},"obj":"Chemical"}],"attributes":[{"id":"A1138","pred":"chebi_id","subj":"T1138","obj":"http://purl.obolibrary.org/obo/CHEBI_17012"},{"id":"A1139","pred":"chebi_id","subj":"T1138","obj":"http://purl.obolibrary.org/obo/CHEBI_49018"},{"id":"A1140","pred":"chebi_id","subj":"T1140","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1141","pred":"chebi_id","subj":"T1140","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1142","pred":"chebi_id","subj":"T1140","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1143","pred":"chebi_id","subj":"T1140","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1144","pred":"chebi_id","subj":"T1140","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1145","pred":"chebi_id","subj":"T1145","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A1146","pred":"chebi_id","subj":"T1146","obj":"http://purl.obolibrary.org/obo/CHEBI_33696"},{"id":"A1147","pred":"chebi_id","subj":"T1147","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A1148","pred":"chebi_id","subj":"T1148","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1149","pred":"chebi_id","subj":"T1148","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1150","pred":"chebi_id","subj":"T1148","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1151","pred":"chebi_id","subj":"T1148","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1152","pred":"chebi_id","subj":"T1148","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1153","pred":"chebi_id","subj":"T1153","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1154","pred":"chebi_id","subj":"T1153","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1155","pred":"chebi_id","subj":"T1153","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1156","pred":"chebi_id","subj":"T1153","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1157","pred":"chebi_id","subj":"T1153","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1158","pred":"chebi_id","subj":"T1158","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1159","pred":"chebi_id","subj":"T1158","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1160","pred":"chebi_id","subj":"T1158","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1161","pred":"chebi_id","subj":"T1158","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1162","pred":"chebi_id","subj":"T1158","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"},{"id":"A1163","pred":"chebi_id","subj":"T1163","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A1164","pred":"chebi_id","subj":"T1164","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A1165","pred":"chebi_id","subj":"T1165","obj":"http://purl.obolibrary.org/obo/CHEBI_35962"},{"id":"A1166","pred":"chebi_id","subj":"T1165","obj":"http://purl.obolibrary.org/obo/CHEBI_38358"},{"id":"A1167","pred":"chebi_id","subj":"T1165","obj":"http://purl.obolibrary.org/obo/CHEBI_45373"},{"id":"A1168","pred":"chebi_id","subj":"T1165","obj":"http://purl.obolibrary.org/obo/CHEBI_74801"},{"id":"A1169","pred":"chebi_id","subj":"T1165","obj":"http://purl.obolibrary.org/obo/CHEBI_26667"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T58","span":{"begin":207,"end":220},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T59","span":{"begin":310,"end":325},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T60","span":{"begin":312,"end":325},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T61","span":{"begin":424,"end":437},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T62","span":{"begin":445,"end":460},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T63","span":{"begin":447,"end":460},"obj":"http://purl.obolibrary.org/obo/GO_0070085"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"LitCovid-sentences","denotations":[{"id":"T359","span":{"begin":0,"end":104},"obj":"Sentence"},{"id":"T360","span":{"begin":105,"end":206},"obj":"Sentence"},{"id":"T361","span":{"begin":207,"end":385},"obj":"Sentence"},{"id":"T362","span":{"begin":386,"end":444},"obj":"Sentence"},{"id":"T363","span":{"begin":445,"end":500},"obj":"Sentence"},{"id":"T364","span":{"begin":501,"end":551},"obj":"Sentence"},{"id":"T365","span":{"begin":552,"end":638},"obj":"Sentence"},{"id":"T366","span":{"begin":639,"end":710},"obj":"Sentence"},{"id":"T367","span":{"begin":711,"end":840},"obj":"Sentence"},{"id":"T368","span":{"begin":841,"end":956},"obj":"Sentence"},{"id":"T369","span":{"begin":957,"end":1008},"obj":"Sentence"},{"id":"T370","span":{"begin":1009,"end":1087},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}

{"project":"2_test","denotations":[{"id":"32604730-16603523-51944020","span":{"begin":202,"end":204},"obj":"16603523"},{"id":"32604730-18396435-51944021","span":{"begin":836,"end":838},"obj":"18396435"},{"id":"T99874","span":{"begin":202,"end":204},"obj":"16603523"},{"id":"T58970","span":{"begin":836,"end":838},"obj":"18396435"}],"text":"In γ-CoVs, IBV strains, known as poultry respiratory infectious pathogens, can agglutinate erythrocytes. IBV prefers to recognize α2,3-NeuAc and the SA functions as a host entry receptor for infection [66]. Glycosylation of IBV M41 S1 protein RBD is crucial for interaction with chicken trachea tissue and RBD N-glycosylation confers receptor specificity and enables virus replication. The heavy glycosylated M41 RBD has 10 glycosylation sites. N-glycosylation of IBV determines receptor specificity. However, the host receptor has not yet been found. NA treatment reduces the binding of soluble S to kidney and tracheal epithelial cells. The IBV S protein recognizes epithelial cells in a SA-dependent manner. The SA-binding ability of IBV is necessary for infection of tracheal epithelial cells and lung respiratory epithelial cells [67]. The SA-binding site is located on S1 of the IBV S protein, although the IBV-specific protein receptor is not known. In contrast to BCoV or HCoV-OC43, IBV lacks an RDE. SA binding of IBV is likely more essential than in other viruses such as TGEV."}