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TitleACE2 utilization of HKU25 clade MERS-related coronaviruses with broad geographic distribution.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateFeb 19, 2025
AuthorsChen Liu / Young-Jun Park / Cheng-Bao Ma / Cameron Stuart / Risako Gen / Yu-Cheng Sun / Xiao Yang / Mei-Yi Lin / Qing Xiong / Jun-Yu Si / Peng Liu / David Veesler / Huan Yan /
PubMed AbstractDipeptidyl peptidase-4 (DPP4) is a well-established receptor for several MERS-related coronaviruses (MERSr-CoVs) isolated from humans, camels, pangolins, and bats (1-6). However, the receptor usage ...Dipeptidyl peptidase-4 (DPP4) is a well-established receptor for several MERS-related coronaviruses (MERSr-CoVs) isolated from humans, camels, pangolins, and bats (1-6). However, the receptor usage of many genetically diverse bat MERSr-CoVs with broad geographical distributions remains poorly understood. Recent studies have identified angiotensin-converting enzyme 2 (ACE2) as an entry receptor for multiple merbecovirus clades. Here, using viral antigen and pseudovirus-based functional assays, we demonstrate that several bat merbecoviruses from the HKU25 clade previously thought to utilize DPP4 (7), employ ACE2 as their functional receptor. Cryo-electron microscopy analysis revealed that HsItaly2011 and VsCoV-a7 recognize ACE2 with a binding mode sharing similarity with that of HKU5 but involving remodeled interfaces and distinct ortholog selectivity, suggesting a common evolutionary origin of ACE2 utilization for these two clades of viruses. EjCoV-3, a strain closely related to the DPP4-using MERSr-CoV BtCoV-422, exhibited relatively broad ACE2 ortholog tropism and could utilize human ACE2 albeit suboptimally. Despite differences in entry mechanisms and spike proteolytic activation compared to MERS-CoV, these viruses remain sensitive to several broadly neutralizing antibodies and entry inhibitors. These findings redefine our understanding of the evolution of receptor usage among MERSr-CoVs and highlight the versatility of ACE2 as a functional receptor for diverse coronaviruses.
External linksbioRxiv / PubMed:40027745 / PubMed Central
MethodsEM (single particle)
Resolution2.5 Å
Structure data

49092

9n7d

EMDB-49092, PDB-9n7d:
Structure of the Rattus norvegicus ACE2 receptor bound HsItaly2011 RBD complex
Method: EM (single particle) / Resolution: 2.5 Å

49093

9n7e

EMDB-49093, PDB-9n7e:
Eptesicus fuscus ACE2 peptidase domain bound to VsCoV-a7 RBD complex
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • merbecovirus
  • rattus norvegicus (Norway rat)
  • eptesicus fuscus (big brown bat)
KeywordsHYDROLASE/VIRAL PROTEIN / HKU25 coronaviruses / MERSr-CoV / Spike glycoprotein / fusion protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / inhibitor / VIRAL PROTEIN-HYDROLASE complex / HYDROLASE-VIRAL PROTEIN complex / Virus / HKU25 clade MERS-related coronaviruses / ACE2 / Glycoprotein / Receptor

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