Abstract

Targeting the SARS-CoV-2 spike The surface of severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2) is decorated with trimeric spikes that bind to host cell receptors. These spikes also elicit an antibody response, so understanding antibody recognition may aid in vaccine design. Yuan et al. determined the structure of CR3022, a neutralizing antibody obtained from a convalescent SARS-CoV–infected patient, in complex with the receptor-binding domain of the SARS-CoV-2 spike. The antibody binds to an epitope conserved between SARS-CoV-2 and SARS-CoV that is distinct from the receptor-binding site. CR3022 likely binds more tightly to SARS-CoV because its epitope contains a glycan not present in SARS-CoV-2. Structural modeling showed that the epitope is only revealed when at least two of the three spike proteins are in a conformation competent to bind the receptor. Science , this issue p. 630

Keywords

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Coronavirus disease 2019 (COVID-19)Sars virus2019-20 coronavirus outbreakEpitopeBiologyComputational biologyBetacoronavirusVirologyGeneticsEvolutionary biologyAntibodyMedicineInfectious disease (medical specialty)

MeSH Terms

Amino Acid SequenceAngiotensin-Converting Enzyme 2AntibodiesNeutralizingAntibodiesViralAntibody AffinityAntigensViralBetacoronavirusBinding SitesCross ReactionsCrystallographyX-RayEpitopesModelsMolecularPeptidyl-Dipeptidase AProtein ConformationProtein DomainsProtein Interaction Domains and MotifsReceptorsCoronavirusReceptorsVirusSevere acute respiratory syndrome-related coronavirusSARS-CoV-2Spike GlycoproteinCoronavirus

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Publication Info

Year
2020
Type
article
Volume
368
Issue
6491
Pages
630-633
Citations
1644
Access
Closed

Social Impact

Social media, news, blog, policy document mentions

Citation Metrics

1644
OpenAlex
122
Influential
1438
CrossRef

Cite This

Meng Yuan, Nicholas C. Wu, Xueyong Zhu et al. (2020). A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. Science , 368 (6491) , 630-633. https://doi.org/10.1126/science.abb7269

Identifiers

DOI
10.1126/science.abb7269
PMID
32245784
PMCID
PMC7164391

Data Quality

Data completeness: 90%