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Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4
Open accessAbstract
The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4). Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction. We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4. Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain. The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain. MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain. Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell. The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
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Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
Raj, V. S., Mou, H., Smits, S. L., Dekkers, D. H. W., Müller, M. A., Dijkman, R., Muth, D., Demmers, J. A. A., Zaki, A., Fouchier, R. A. M., et al. (2013) · Nature · doi:10.1038/nature12005 · Cited by 2,061
Coronavirus Pathogenesis and the Emerging Pathogen Severe Acute Respiratory Syndrome Coronavirus
Weiss, S. R., & Navas-Martin, S. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.4.635-664.2005 · Cited by 1,256 · cited 2×
“The S glycoprotein consists of a globular S1 domain at the N-terminal region, followed by membrane-proximal S2 domain, a transmembrane domain and an intracellular domain [11] [12] [13] .”
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Lu, R., Zhao, X., Li, J., Niu, P., Yang, B., Wu, H., Wang, W., Song, H., Huang, B., Zhu, N., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30251-8 · Cited by 11,907
Self-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
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Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073
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Hu, B., Ge, X., Wang, L.-F., & Shi, Z. (2015) · Virology Journal · doi:10.1186/s12985-015-0422-1 · Cited by 344
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Du, L., Yang, Y., Zhou, Y., Lu, L., Li, F., & Jiang, S. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1271415 · Cited by 301
Scobey, T., Yount, B. L., Sims, A. C., Donaldson, E. F., Agnihothram, S. S., Menachery, V. D., Graham, R. L., Swanstrom, J., Bove, P. F., Kim, J. D., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311542110 · Cited by 283
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Glasgow, A., Glasgow, J., Limonta, D., Solomon, P., Lui, I., Zhang, Y., Nix, M. A., Rettko, N. J., Zha, S., Yamin, R., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016093117 · Cited by 251
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Natoli, S., Oliveira, V., Calabresi, P., Maia, L. F., & Pisani, A. (2020) · European Journal of Neurology · doi:10.1111/ene.14277 · Cited by 260
Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors
Park, Y.-J., Walls, A. C., Wang, Z., Sauer, M. M., Li, W., Tortorici, M. A., Bosch, B.-J., DiMaio, F., & Veesler, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0334-7 · Cited by 260
Tang, X.-C., Agnihothram, S. S., Jiao, Y., Stanhope, J., Graham, R. L., Peterson, E. C., Avnir, Y., Tallarico, A. S. C., Sheehan, J., Zhu, Q., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402074111 · Cited by 232
Corti, D., Zhao, J., Pedotti, M., Simonelli, L., Agnihothram, S., Fett, C., Fernandez-Rodriguez, B., Foglierini, M., Agatic, G., Vanzetta, F., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510199112 · Cited by 216
Wang, L., Shi, W., Chappell, J. D., Joyce, M. G., Zhang, Y., Kanekiyo, M., Becker, M. M., van Doremalen, N., Fischer, R., Wang, N., et al. (2018) · Journal of Virology · doi:10.1128/jvi.02002-17 · Cited by 169
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Wang, N., Rosen, O., Wang, L., Turner, H. L., Stevens, L. J., Corbett, K. S., Bowman, C. A., Pallesen, J., Shi, W., Zhang, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.052 · Cited by 86
Self-citationChen, Y., Lu, S., Jia, H., Deng, Y., Zhou, J., Huang, B., Yu, Y., Lan, J., Wang, W., Lou, Y., et al. (2017) · Emerging Microbes & Infections · doi:10.1038/emi.2017.50 · Cited by 81
Self-citationEmergence of bat-related betacoronaviruses: hazard and risks
Frutos, R., Serra-Cobo, J., Pinault, L., Lopez Roig, M., & Devaux, C. A. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.591535 · Cited by 66
Dong, T. N., Brogden, G., Gerold, G., & Khosla, M. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04484-y · Cited by 39
Ahmed-Hassan, H., Sisson, B., Shukla, R. K., Wijewantha, Y., Funderburg, N. T., Li, Z., Hayes, D., Demberg, T., & Liyanage, N. P. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01979 · Cited by 47
Metadata
- Authors
- Wang, N., Shi, X., Jiang, L., Zhang, S., Wang, D., Tong, P., Guo, D., Fu, L., Cui, Y., Liu, X., Arledge, K. C., Chen, Y.-H., Zhang, L., & Wang, X.
- Venue
- Cell Research
- Published
- 2013-07-09
- Volume
- 23
- Issue
- 8
- Pages
- 986-993
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- OpenAlex
- W2013090907
- Cited by
- 719
- References
- 5
- FWCI
- 24.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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