The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
Open accessAbstract
The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.
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Cited by
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
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Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
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Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
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Metadata
- Authors
- Yuan, Y., Cao, D., Zhang, Y., Ma, J., Qi, J., Wang, Q., Lu, G., Wu, Y., Yan, J., Shi, Y., Zhang, X., & Gao, G. F.
- Venue
- Nature Communications
- Published
- 2017-04-10
- Volume
- 8
- Issue
- 1
- Pages
- 15092-15092
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2606148195
- Cited by
- 760
- References
- 48
- FWCI
- 65.41
- Type
- journal article
- Language
- en
- Open access
- gold
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