Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, Jason S. McLellan
Summary
The authors determined a 3.5 angstrom cryo-EM structure of the SARS-CoV-2 (2019-nCoV) spike glycoprotein ectodomain stabilized in the prefusion conformation. They showed the receptor-binding domain engages human ACE2 with roughly 10- to 20-fold higher affinity than the SARS-CoV-1 spike, helping explain efficient human transmission. They also found that SARS-CoV-1 receptor-binding antibodies did not appreciably bind the new spike, informing vaccine and therapeutic design.
Key findings
- Solved a 3.5 angstrom prefusion cryo-EM structure of the SARS-CoV-2 spike ectodomain.
- Measured high-affinity binding of the spike to ACE2, exceeding SARS-CoV-1 spike affinity.
- Demonstrated limited cross-reactivity of SARS-CoV-1 antibodies, with implications for vaccine design.
Subjects & keywords
Cite this paper
Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett, Jory A. Goldsmith, Ching-Lin Hsieh, Olubukola Abiona, Barney S. Graham, & Jason S. McLellan (2020). Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. https://doi.org/10.1126/science.abb2507
@article{wrapp2020cryoem,
author = {Daniel Wrapp and Nianshuang Wang and Kizzmekia S. Corbett and Jory A. Goldsmith and Ching-Lin Hsieh and Olubukola Abiona and Barney S. Graham and Jason S. McLellan},
title = {Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation},
journal = {Science},
year = {2020},
doi = {10.1126/science.abb2507},
url = {https://doi.org/10.1126/science.abb2507}
}