Service interruption on Monday 11 July from 12:30 to 13:00: all the sites of the CCSD (HAL, Epiciences, SciencesConf, AureHAL) will be inaccessible (network hardware connection).
Skip to Main content Skip to Navigation
Journal articles

Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer

Abstract : The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions. S also contains the principal antigenic determinants and is the target of neutralizing antibodies. Here we present the structure of a mouse coronavirus S trimer ectodomain determined at 4.0 Å resolution by single particle cryo-electron microscopy. It reveals the metastable pre-fusion architecture of S and highlights key interactions stabilizing it. The structure shares a common core with paramyxovirus F proteins, implicating mechanistic similarities and an evolutionary connection between these viral fusion proteins. The accessibility of the highly conserved fusion peptide at the periphery of the trimer indicates potential vaccinology strategies to elicit broadly neutralizing antibodies against coronaviruses. Finally, comparison with crystal structures of human coronavirus S domains allows rationalization of the molecular basis for species specificity based on the use of spatially contiguous but distinct domains.
Document type :
Journal articles
Complete list of metadata
Contributor : M. Alejandra Tortorici Connect in order to contact the contributor
Submitted on : Thursday, December 14, 2017 - 5:22:31 PM
Last modification on : Friday, May 6, 2022 - 2:54:40 PM

Links full text




Alexandra Walls, M. Alejandra Tortorici, Berend-Jan Bosch, Brandon Frenz, Peter J. M. Rottier, et al.. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature, Nature Publishing Group, 2016, 531 (7592), pp.114 - 117. ⟨10.1038/nature16988⟩. ⟨pasteur-01664346⟩



Record views