1. Crystal Structure of the Receptor-Binding Domain from Newly Emerged Middle East Respiratory Syndrome Coronavirus.
- Author
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Yaoqing Chen, Rajashankar, Kanagalaghatta R., Yang Yang, Agnihothram, Sudhakar S., Chang Liu, Yi-Lun Lin, Baric, Ralph S., and Fang Li
- Subjects
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CRYSTAL structure , *RADIOLIGAND assay , *MERS coronavirus , *INFECTIOUS disease transmission , *CORONAVIRUS diseases - Abstract
The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans. [ABSTRACT FROM AUTHOR]
- Published
- 2013
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