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J Virol. 2013 Oct;87(19):10777-83. doi: 10.1128/JVI.01756-13. Epub 2013 Jul 31.

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus.

Author information

1
Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, USA.

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.

PMID:
23903833
PMCID:
PMC3807420
DOI:
10.1128/JVI.01756-13
[Indexed for MEDLINE]
Free PMC Article

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