6533b836fe1ef96bd12a136c
RESEARCH PRODUCT
In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges
Sören Von BülowMichael D. MühlebachAndre SchwarzSonja WelschNayara Trevisan Doimo De AzevedoGer Van ZandbergenGer Van ZandbergenFlorian BlancShyamal MosalagantiShyamal MosalagantiJonathan J M LandryKatrin BagolaMartin BeckMartin BeckWim J. H. HagenMateusz SikoraChristoph SchürmannCindy HörnerRoberto CovinoRoberto CovinoMichael GechtJacomine Krijnse LockerGerhard HummerGerhard HummerBeata TuroňováBeata Turoňovásubject
In situElectron Microscope TomographyGlycanGlycosylationFlexibility (anatomy)virusesProtein domainPneumonia ViralHingeMolecular Dynamics SimulationBiologylaw.inventionBetacoronavirusProtein DomainslawTarget identificationmedicineHumansPandemicsResearch ArticlesHost cell surfaceMultidisciplinarySARS-CoV-2R-ArticlesCryoelectron MicroscopyBiochemCOVID-19MicrobioResearch HighlightCell biologymedicine.anatomical_structureSpike Glycoprotein Coronavirusbiology.proteinRecombinant DNASpike (software development)Protein MultimerizationStructural biologyCoronavirus InfectionsResearch Articledescription
Flexible spikes The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein enables viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor and is a major target for neutralizing antibodies. About 20 to 40 spikes decorate the surface of virions. Turoňová et al. now show that the spike is flexibly connected to the viral surface by three hinges that are well protected by glycosylation sites. The flexibility imparted by these hinges may explain how multiple spikes act in concert to engage onto the flat surface of a host cell. Science, this issue p. 203
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-08-01 | Science (New York, N.y.) |