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Novel ACE2 binding in bat merbecoviruses expands potential host range.
Xiaoguang Zhang1, Xing Ma1, Ye Chen2
1Academy for Advanced Interdisciplinary Studies, Engineering Laboratory of Animal Immunity of Jiangsu Province, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
Plos Pathogens
|November 11, 2025
Summary
This study reveals how bat merbecoviruses bind to ACE2 receptors, with some viruses showing broad host ranges, including potential intermediate hosts like mink and pangolins, highlighting zoonotic transmission risks.
Area of Science:
- Virology
- Molecular Biology
- Ecology
Background:
- Coronaviruses exhibit host specificity determined by receptor binding, influencing zoonotic potential.
- Merbecoviruses (e.g., MERS-CoV) use DPP4, while Sarbecoviruses (e.g., SARS-CoV) use ACE2.
- Bat-borne merbecoviruses pose potential zoonotic threats.
Purpose of the Study:
- To investigate the ACE2 receptor usage of four bat merbecoviruses: HKU5, BtVs-SC2013, HKU25, and P. khulii-2011.
- To elucidate the molecular mechanisms underlying species-specific ACE2 binding and host adaptation.
- To assess the potential for cross-species transmission to non-bat hosts.
Main Methods:
- Species-specific ACE2 binding assays for bat merbecoviruses.
- Structural analysis and site-directed mutagenesis of ACE2-RBD interactions.
- Investigation of glycosylation site impact on receptor binding.
Main Results:
- HKU5 exhibits exclusive binding to Pipistrellus abramus ACE2, while P. khulii-2011 binds only to Murina aurata ACE2.
- BtVs-SC2013 binds to Murina aurata and Myotis myotis ACE2, and also to mink ACE2.
- HKU25 demonstrates broad ACE2 binding, including pangolin and mink ACE2, suggesting potential intermediate hosts.
- A specific N-glycosylation site on P. abramus ACE2 is critical for HKU5 binding; its modification affects binding.
- Key residues in mink ACE2 were identified for BtVs-SC2013 and HKU25 binding.
Conclusions:
- Bat merbecoviruses display diverse ACE2 receptor tropisms and host specificities.
- The binding mechanisms involve specific ACE2 residues and glycosylation patterns.
- Findings enhance understanding of bat merbecovirus evolution and zoonotic spillover potential.
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