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Article: Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

TitleStructural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Authors
KeywordsSARS-CoV-2
CTD
receptor binding domain
receptor
ACE2
Issue Date2020
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/cell
Citation
Cell, 2020, v. 181, p. 894-904.e9 How to Cite?
AbstractThe recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.
Persistent Identifierhttp://hdl.handle.net/10722/289788
ISSN
2020 Impact Factor: 41.582
2020 SCImago Journal Rankings: 26.304
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWang, Q-
dc.contributor.authorZhang, Y-
dc.contributor.authorWu, L-
dc.contributor.authorNiu, C-
dc.contributor.authorSong, C-
dc.contributor.authorZhang, Z-
dc.contributor.authorLu, G-
dc.contributor.authorQiao, C-
dc.contributor.authorHu, Y-
dc.contributor.authorYuen, KY-
dc.contributor.authorWang, Q-
dc.contributor.authorZhou, H-
dc.contributor.authorYan, J-
dc.contributor.authorQi, J-
dc.date.accessioned2020-10-22T08:17:29Z-
dc.date.available2020-10-22T08:17:29Z-
dc.date.issued2020-
dc.identifier.citationCell, 2020, v. 181, p. 894-904.e9-
dc.identifier.issn0092-8674-
dc.identifier.urihttp://hdl.handle.net/10722/289788-
dc.description.abstractThe recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.-
dc.languageeng-
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/cell-
dc.relation.ispartofCell-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectSARS-CoV-2-
dc.subjectCTD-
dc.subjectreceptor binding domain-
dc.subjectreceptor-
dc.subjectACE2-
dc.titleStructural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2-
dc.typeArticle-
dc.identifier.emailYuen, KY: kyyuen@hkucc.hku.hk-
dc.identifier.authorityYuen, KY=rp00366-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1016/j.cell.2020.03.045-
dc.identifier.pmid32275855-
dc.identifier.pmcidPMC7144619-
dc.identifier.scopuseid_2-s2.0-85083338073-
dc.identifier.hkuros317217-
dc.identifier.volume181-
dc.identifier.spage894-
dc.identifier.epage904.e9-
dc.identifier.isiWOS:000533623900014-
dc.publisher.placeUnited States-
dc.identifier.issnl0092-8674-

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