PMC:7712180 / 48006-49316 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"1561","span":{"begin":102,"end":106},"obj":"Gene"},{"id":"1562","span":{"begin":206,"end":210},"obj":"Gene"},{"id":"1563","span":{"begin":323,"end":327},"obj":"Gene"},{"id":"1564","span":{"begin":1249,"end":1252},"obj":"Gene"},{"id":"1565","span":{"begin":392,"end":401},"obj":"Species"},{"id":"1566","span":{"begin":416,"end":419},"obj":"Species"},{"id":"1567","span":{"begin":437,"end":440},"obj":"Species"},{"id":"1568","span":{"begin":668,"end":677},"obj":"Species"},{"id":"1569","span":{"begin":695,"end":698},"obj":"Species"},{"id":"1570","span":{"begin":753,"end":756},"obj":"Species"},{"id":"1571","span":{"begin":1011,"end":1015},"obj":"Species"},{"id":"1572","span":{"begin":1234,"end":1239},"obj":"Species"},{"id":"1573","span":{"begin":1243,"end":1248},"obj":"Species"},{"id":"1574","span":{"begin":411,"end":415},"obj":"Species"},{"id":"1575","span":{"begin":432,"end":436},"obj":"Species"},{"id":"1576","span":{"begin":690,"end":694},"obj":"Species"},{"id":"1577","span":{"begin":748,"end":752},"obj":"Species"},{"id":"1578","span":{"begin":1006,"end":1010},"obj":"Species"},{"id":"1579","span":{"begin":138,"end":147},"obj":"Chemical"},{"id":"1580","span":{"begin":860,"end":868},"obj":"Chemical"},{"id":"1581","span":{"begin":39,"end":46},"obj":"Mutation"},{"id":"1582","span":{"begin":221,"end":226},"obj":"Mutation"},{"id":"1583","span":{"begin":279,"end":284},"obj":"Mutation"}],"attributes":[{"id":"A1561","pred":"tao:has_database_id","subj":"1561","obj":"Gene:290"},{"id":"A1562","pred":"tao:has_database_id","subj":"1562","obj":"Gene:290"},{"id":"A1563","pred":"tao:has_database_id","subj":"1563","obj":"Gene:290"},{"id":"A1564","pred":"tao:has_database_id","subj":"1564","obj":"Gene:290"},{"id":"A1565","pred":"tao:has_database_id","subj":"1565","obj":"Tax:11137"},{"id":"A1566","pred":"tao:has_database_id","subj":"1566","obj":"Tax:11118"},{"id":"A1567","pred":"tao:has_database_id","subj":"1567","obj":"Tax:11118"},{"id":"A1568","pred":"tao:has_database_id","subj":"1568","obj":"Tax:11137"},{"id":"A1569","pred":"tao:has_database_id","subj":"1569","obj":"Tax:11118"},{"id":"A1570","pred":"tao:has_database_id","subj":"1570","obj":"Tax:11118"},{"id":"A1571","pred":"tao:has_database_id","subj":"1571","obj":"Tax:11118"},{"id":"A1572","pred":"tao:has_database_id","subj":"1572","obj":"Tax:9838"},{"id":"A1573","pred":"tao:has_database_id","subj":"1573","obj":"Tax:9606"},{"id":"A1574","pred":"tao:has_database_id","subj":"1574","obj":"Tax:11137"},{"id":"A1575","pred":"tao:has_database_id","subj":"1575","obj":"Tax:11137"},{"id":"A1576","pred":"tao:has_database_id","subj":"1576","obj":"Tax:11137"},{"id":"A1577","pred":"tao:has_database_id","subj":"1577","obj":"Tax:11137"},{"id":"A1578","pred":"tao:has_database_id","subj":"1578","obj":"Tax:11137"},{"id":"A1579","pred":"tao:has_database_id","subj":"1579","obj":"MESH:D004220"},{"id":"A1580","pred":"tao:has_database_id","subj":"1580","obj":"MESH:D006859"},{"id":"A1581","pred":"tao:has_standard_notation","subj":"1581","obj":"c.317C\u003eS,C"},{"id":"A1582","pred":"tao:has_standard_notation","subj":"1582","obj":"p.F318A"},{"id":"A1583","pred":"tao:has_standard_notation","subj":"1583","obj":"p.N319A"}],"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":"Mutagenesis of class I revealed that a C317S/C320S double mutation within loop 1 abolished binding to hAPN, suggesting that the C317-C320 disulfide bond is important for loop 1 folding and interaction with hAPN. While an F318A mutant showed a 13-fold reduction in affinity, both N319A and W404A mutations lead to a loss of hAPN binding [83]. Alignment of the RBS aa sequences of 6 classes of HCoV-229E with bat-229E CoV and camelid-229E CoV (Figure 7c) showed that 6 amino acids, F308, G313, G315, C317, C320 and N319 (based on class I numbering), are highly conserved among different classes and hosts. V351 and R359 are conserved in respiratory-transmitted viruses, HCoV-229E and camelid-229E CoV, but not in an oral-fecal-transmitted virus, bat-229E CoV. Amino acids at positions of K/R316, F/Y318 and N319 were observed in all 4 crystal structures to form hydrogen bonds with the receptor, principally stabilizing viral-receptor interactions (Figure 7d). However, the observation that bat- and camelid-229E CoVs contain S/T with a polar uncharged side chain instead of K/R316 with a longer charged side chain suggests that the amino acid at this position may be responsible for the change in receptor binding specificity from bat/camel to human APN receptors that is required for interspecies transmission."}

{"project":"LitCovid-sentences","denotations":[{"id":"T258","span":{"begin":0,"end":211},"obj":"Sentence"},{"id":"T259","span":{"begin":212,"end":341},"obj":"Sentence"},{"id":"T260","span":{"begin":342,"end":603},"obj":"Sentence"},{"id":"T261","span":{"begin":604,"end":757},"obj":"Sentence"},{"id":"T262","span":{"begin":758,"end":958},"obj":"Sentence"},{"id":"T263","span":{"begin":959,"end":1310},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Mutagenesis of class I revealed that a C317S/C320S double mutation within loop 1 abolished binding to hAPN, suggesting that the C317-C320 disulfide bond is important for loop 1 folding and interaction with hAPN. While an F318A mutant showed a 13-fold reduction in affinity, both N319A and W404A mutations lead to a loss of hAPN binding [83]. Alignment of the RBS aa sequences of 6 classes of HCoV-229E with bat-229E CoV and camelid-229E CoV (Figure 7c) showed that 6 amino acids, F308, G313, G315, C317, C320 and N319 (based on class I numbering), are highly conserved among different classes and hosts. V351 and R359 are conserved in respiratory-transmitted viruses, HCoV-229E and camelid-229E CoV, but not in an oral-fecal-transmitted virus, bat-229E CoV. Amino acids at positions of K/R316, F/Y318 and N319 were observed in all 4 crystal structures to form hydrogen bonds with the receptor, principally stabilizing viral-receptor interactions (Figure 7d). However, the observation that bat- and camelid-229E CoVs contain S/T with a polar uncharged side chain instead of K/R316 with a longer charged side chain suggests that the amino acid at this position may be responsible for the change in receptor binding specificity from bat/camel to human APN receptors that is required for interspecies transmission."}