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http://purl.uniprot.org/citations/36640338http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36640338http://www.w3.org/2000/01/rdf-schema#comment"The BA.2 sub-lineage of the Omicron (B.1.1.529) severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant rapidly supplanted the original BA.1 sub-lineage in early 2022. Both lineages threatened the efficacy of vaccine-elicited antibodies and acquired increased binding to several mammalian ACE2 receptors. Cryoelectron microscopy (cryo-EM) analysis of the BA.2 spike (S) glycoprotein in complex with mouse ACE2 (mACE2) identifies BA.1- and BA.2-mutated residues Q493R, N501Y, and Y505H as complementing non-conserved residues between human and mouse ACE2, rationalizing the enhanced S protein-mACE2 interaction for Omicron variants. Cryo-EM structures of the BA.2 S-human ACE2 complex and of the extensively mutated BA.2 amino-terminal domain (NTD) reveal a dramatic reorganization of the highly antigenic N1 loop into a β-strand, providing an explanation for decreased binding of the BA.2 S protein to antibodies isolated from BA.1-convalescent patients. Our analysis reveals structural mechanisms underlying the antigenic drift in the rapidly evolving Omicron variant landscape."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2022.111964"xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Subramaniam S."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Zhu X."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Berezuk A.M."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Mannar D."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Saville J.W."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Tuttle K.S."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Cholak S."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/author"Vahdatihassani F."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/name"Cell Rep"xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/pages"111964"xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/title"Structural analysis of receptor engagement and antigenic drift within the BA.2 spike protein."xsd:string
http://purl.uniprot.org/citations/36640338http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/36640338http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36640338
http://purl.uniprot.org/citations/36640338http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36640338
http://purl.uniprot.org/uniprot/#_P0DTC2-mappedCitation-36640338http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36640338
http://purl.uniprot.org/uniprot/#_Q9BYF1-mappedCitation-36640338http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36640338
http://purl.uniprot.org/uniprot/#_Q8R0I0-mappedCitation-36640338http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36640338
http://purl.uniprot.org/uniprot/Q8R0I0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36640338
http://purl.uniprot.org/uniprot/Q9BYF1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36640338
http://purl.uniprot.org/uniprot/P0DTC2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/36640338