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    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.


    Nianshuang Wang, Xuanling Shi, Liwei Jiang, Senyan Zhang, Dongli Wang, Pei Tong, Dongxing Guo, Lili Fu, Ye Cui, Xi Liu, Kelly C Arledge, Ying-Hua Chen, Linqi Zhang, Xinquan Wang. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell research. 2013 Aug;23(8):986-93

    PMID: 23835475

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