A MERS-CoV-like mink coronavirus uses ACE2 as an entry receptor

Ningning Wang, Weiwei Ji, Houqi Jiao, Michael Veit, Ju Sun, Yanjun Wang, Xing Ma, Yu Wang, Yutong Wang, Xin-xin Li, Xiaoguang Zhang, Jie Chen, Jiayu Wei, Ying Xu, Dawei Guo, Xiaofeng Zhai, Andres Merits, Chang Li, Félix A. Rey, Georgi M. Dobrikov, George F. Gao, Shuijun Zhang (), Yuhai Bi () and Shuo Su ()
Additional contact information
Ningning Wang: Nanjing Agricultural University
Weiwei Ji: Nanjing Agricultural University
Houqi Jiao: Nanjing Agricultural University
Michael Veit: Free University Berlin
Ju Sun: Chinese Academy of Sciences
Yanjun Wang: Chinese Academy of Sciences
Xing Ma: Nanjing Agricultural University
Yu Wang: Nanjing Agricultural University
Yutong Wang: Nanjing Agricultural University
Xin-xin Li: Nanjing Agricultural University
Xiaoguang Zhang: Nanjing Agricultural University
Jie Chen: Nanjing Agricultural University
Jiayu Wei: Nanjing Agricultural University
Ying Xu: Nanjing Agricultural University
Dawei Guo: Nanjing Agricultural University
Xiaofeng Zhai: Nanjing Agricultural University
Andres Merits: University of Tartu
Chang Li: Chinese Academy of Agricultural Sciences
Félix A. Rey: CNRS UMR 3569
Georgi M. Dobrikov: Bulgarian Academy of Sciences
George F. Gao: Chinese Academy of Sciences
Shuijun Zhang: Nanjing Agricultural University
Yuhai Bi: Chinese Academy of Sciences
Shuo Su: Nanjing Agricultural University

Nature, 2025, vol. 642, issue 8068, 739-746

Abstract: Abstract Despite accumulating evidence that bat-derived coronaviruses often require intermediate hosts to facilitate transmission to humans1, the potential role of fur animals in zoonotic coronavirus spillovers has largely been overlooked2. Here we report the isolation and characterization of a previously undescribed mink respiratory coronavirus (MRCoV) from farmed minks with pneumonia. Notably, MRCoV uses angiotensin-converting enzyme 2 (ACE2) as an entry receptor and can infect mink, bat, monkey and human cells. Cryo-electron microscopy analyses revealed that the MRCoV receptor-binding domain (RBD) binds to the same interface on ACE2 receptors as the RBD of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) despite structural differences. We identify the key determinants on the RBD of MRCoV and ACE2 that confer efficient binding. HKU5-33S, a bat coronavirus closely related to MRCoV, uses ACE2 of the bat Pipistrellus abramus for cell entry and requires only two amino acid substitutions to adapt to mink ACE2. SARS-CoV-2 protease and polymerase inhibitors potently block MRCoV infection, thereby indicating a potential therapeutic strategy. Collectively, these findings enhance our understanding of coronavirus receptor dynamics and highlight their zoonotic potential. Given the risks posed by fur farms as reservoirs for emerging pathogens, our study underscores the need for enhanced surveillance to mitigate future coronavirus outbreaks.

Date: 2025
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DOI: 10.1038/s41586-025-09007-w

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