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Article: A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV

TitleA highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Authors
Keywordsamino terminal sequence
antibody isolation
antigen bindingantigenicityArticlebinding affinity
Issue Date2020
PublisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.org
Citation
Science, 2020, v. 368 n. 6491, p. 630-633 How to Cite?
AbstractThe outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.
Persistent Identifierhttp://hdl.handle.net/10722/289111
ISSN
2020 Impact Factor: 47.728
2020 SCImago Journal Rankings: 12.556
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYuan, M-
dc.contributor.authorWu, NC-
dc.contributor.authorZhu, X-
dc.contributor.authorLee, CCD-
dc.contributor.authorSO, RTY-
dc.contributor.authorLyu, H-
dc.contributor.authorMok, CKP-
dc.contributor.authorWilson, IA-
dc.date.accessioned2020-10-22T08:07:58Z-
dc.date.available2020-10-22T08:07:58Z-
dc.date.issued2020-
dc.identifier.citationScience, 2020, v. 368 n. 6491, p. 630-633-
dc.identifier.issn0036-8075-
dc.identifier.urihttp://hdl.handle.net/10722/289111-
dc.description.abstractThe outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.-
dc.languageeng-
dc.publisherAmerican Association for the Advancement of Science. The Journal's web site is located at http://sciencemag.org-
dc.relation.ispartofScience-
dc.rightsScience. Copyright © American Association for the Advancement of Science.-
dc.rightsThis is the author’s version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in [Science Journal Title] on [Volume number and date], DOI: [insert DOI number].-
dc.subjectamino terminal sequence-
dc.subjectantibody isolation-
dc.subjectantigen bindingantigenicityArticlebinding affinity-
dc.titleA highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV-
dc.typeArticle-
dc.identifier.emailMok, CKP: ch02mkp@hkucc.hku.hk-
dc.identifier.authorityMok, CKP=rp01805-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1126/science.abb7269-
dc.identifier.pmid32245784-
dc.identifier.pmcidPMC7164391-
dc.identifier.scopuseid_2-s2.0-85084612296-
dc.identifier.hkuros317041-
dc.identifier.volume368-
dc.identifier.issue6491-
dc.identifier.spage630-
dc.identifier.epage633-
dc.identifier.isiWOS:000531182900061-
dc.publisher.placeUnited States-
dc.identifier.issnl0036-8075-

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