The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
Open accessAbstract
The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans, representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus–cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 β-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein–protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among betacoronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition.
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Cited by
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Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
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“In light of the determinant role of SARS-RBD and MERS-RBD in receptor recognition (Li et al., 2003, 2005; Lu et al., 2013; Raj et al., 2013), the majority of neutralizing antibodies have been shown to target the RBD, exerting neutralization activity by disrupting virus/receptor engagement (Du et al.”
InfluentialSelf-citationOu, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022
Metadata
- Authors
- Lu, G., Hu, Y., Wang, Q., Qi, J., Gao, F., Li, Y., Zhang, Y., Zhang, W., Yuan, Y., Bao, J., Zhang, B., Shi, Y., Yan, J., & Gao, G. F.
- Venue
- Nature
- Published
- 2013-07-07
- Volume
- 500
- Issue
- 7461
- Pages
- 227-231
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2120967846
- Cited by
- 739
- References
- 6
- FWCI
- 34.78
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Lu, G., Hu, Y., Wang, Q., Qi, J., Gao, F., Li, Y., Zhang, Y., Zhang, W., Yuan, Y., Bao, J., Zhang, B., Shi, Y., Yan, J., & Gao, G. F. (2013). Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature. https://doi.org/10.1038/nature12328
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