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Structure paper

TitleMolecular basis of convergent evolution of ACE2 receptor utilization among HKU5 coronaviruses.
Journal, issue, pagesCell, Vol. 188, Issue 6, Page 1711-1728.e21, Year 2025
Publish dateMar 20, 2025
AuthorsYoung-Jun Park / Chen Liu / Jimin Lee / Jack T Brown / Cheng-Bao Ma / Peng Liu / Risako Gen / Qing Xiong / Samantha K Zepeda / Cameron Stewart / Amin Addetia / Caroline J Craig / M Alejandra Tortorici / Abeer N Alshukairi / Tyler N Starr / Huan Yan / David Veesler /
PubMed AbstractDPP4 was considered a canonical receptor for merbecoviruses until the recent discovery of African bat-borne MERS-related coronaviruses using ACE2. The extent and diversity of ACE2 utilization among ...DPP4 was considered a canonical receptor for merbecoviruses until the recent discovery of African bat-borne MERS-related coronaviruses using ACE2. The extent and diversity of ACE2 utilization among merbecoviruses and their receptor species tropism remain unknown. Here, we reveal that HKU5 enters host cells utilizing Pipistrellus abramus (P.abr) and several non-bat mammalian ACE2s through a binding mode distinct from that of any other known ACE2-using coronaviruses. We defined the molecular determinants of receptor species tropism and identified a single amino acid mutation enabling HKU5 to utilize human ACE2, providing proof of principle for machine-learning-assisted outbreak preparedness. We show that MERS-CoV and HKU5 have markedly distinct antigenicity and identified several HKU5 inhibitors, including two clinical compounds. Our findings profoundly alter our understanding of coronavirus evolution, as several merbecovirus clades independently evolved ACE2 utilization, and pave the way for developing countermeasures against viruses poised for human emergence.
External linksCell / PubMed:39922192
MethodsEM (single particle)
Resolution2.0 - 3.1 Å
Structure data

46512

9d32

EMDB-46512, PDB-9d32:
Structure of the HKU5 RBD bound to the P. abramus ACE2 receptor
Method: EM (single particle) / Resolution: 3.1 Å

47358

9e0i

EMDB-47358, PDB-9e0i:
Structure of the HKU5-19s RBD bound to the Bos taurus ACE2 receptor
Method: EM (single particle) / Resolution: 2.4 Å

47823

9ea0

EMDB-47823, PDB-9ea0:
Structure of the prefusion HKU5-19s Spike trimer (conformation 1)
Method: EM (single particle) / Resolution: 2.0 Å

48048

9eh8

EMDB-48048, PDB-9eh8:
Structure of the prefusion HKU5-19s Spike trimer (conformation 2)
Method: EM (single particle) / Resolution: 2.0 Å

Chemicals

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

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-FOL:
FOLIC ACID

ChemComp-EIC:
LINOLEIC ACID

Source
  • Homo sapiens (human)
  • pipistrellus abramus (Japanese house bat)
  • pipistrellus bat coronavirus hku5
  • bos taurus (domestic cattle)
KeywordsVIRAL PROTEIN/HYDROLASE / MERS-related HKU5 coronaviruses / MERSr-CoV / Spike glycoprotein / fusion protein / Pipistrellus abramus ACE2 / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / inhibitor / VIRAL PROTEIN-HYDROLASE complex / VIRAL PROTEIN / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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