Structural basis for human DPP4 receptor recognition by a pangolin MERS-like coronavirus

文献类型: 外文期刊

第一作者: Yang, Mo

作者: Yang, Mo;Li, Zehou;Xu, Ying;Ji, Weiwei;Li, Xiaoxia;Wei, Jiayu;Zhou, Zhengrong;Ren, Minjie;Ma, Ke;Guan, Jiayu;Mo, Guoxiang;Zhang, Shuijun;Chen, Jing;Li, Yang;Wang, Meihua;Shu, Bo;Shi, Zheng-Li;Xu, Ran;Guo, Jingjing;Chen, Rong;Zhou, Peng;Yuan, Yuan

作者机构:

期刊名称:PLOS PATHOGENS ( 影响因子:4.9; 五年影响因子:5.4 )

ISSN: 1553-7366

年卷期: 2024 年 20 卷 11 期

页码:

收录情况: SCI

摘要: Middle East respiratory syndrome coronavirus (MERS-CoV) and the pangolin MERS-like coronavirus MjHKU4r-CoV-1 employ dipeptidyl peptidase 4 (DPP4) as an entry receptor. MjHKU4r-CoV-1 could infect transgenic mice expressing human DPP4. To understand the mechanism of MjHKU4r-CoV-1 entry into cells, we determined the crystal structures of the receptor binding domain (RBD) of MjHKU4r-CoV-1 spike protein bound to human DPP4 (hDPP4) and Malayan pangolin DPP4 (MjDPP4), respectively. The overall hDPP4-binding mode of MjHKU4r-CoV-1 RBD is similar to that of MERS-CoV RBD. MjHKU4r-CoV-1 RBD shows higher binding affinity to hDPP4 compared to the bat MERS-like coronavirus Ty-BatCoV-HKU4. Via swapping residues between MjHKU4r-CoV-1 RBD and Ty-BatCoV-HKU4 RBD, we identified critical determinants on MjHKU4r-CoV-1 that are responsible for virus usage of hDPP4. Our study suggests that MjHKU4r-CoV-1 is more adapted to the human receptor compared to the bat HKU4 coronavirus and highlights the potential of virus emergence into the human population.

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