ArticleEMBO reports2024
Molecular basis for receptor recognition and broad host tropism for merbecovirus MjHKU4r-CoV-1.
Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural basis for human DPP4 receptor recognition by MERS-like coronaviruses 2014-422 and GX2012.PLoS pathogens · 2026Article
- Structures and receptor binding activities of merbecovirus spike proteins reveal key signatures for human DPP4 adaptation.Science advances · 2025Article
- Designing Sandwich ELISA with Broadly Reactive Anti-Nucleocapsid Monoclonal Antibodies to Detect Bat-Borne Merbecoviruses.Viruses · 2025Article
- Structural basis for human DPP4 receptor recognition by a pangolin MERS-like coronavirus.PLoS pathogens · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
A novel pangolin-origin MERS-like coronavirus (CoV), MjHKU4r-CoV-1, was recently identified. It is closely related to bat HKU4-CoV, and is infectious in human organs and transgenic mice. MjHKU4r-CoV-1 uses the dipeptidyl peptidase 4 (DPP4 or CD26) receptor for virus entry and has a broad host tropism. However, the molecular mechanism of its receptor binding and determinants of host range are not yet clear. Herein, we determine the structure of the MjHKU4r-CoV-1 spike (S) protein receptor-binding domain (RBD) complexed with human CD26 (hCD26) to reveal the basis for its receptor binding. Measuring binding capacity toward multiple animal receptors for MjHKU4r-CoV-1, mutagenesis analyses, and homology modeling highlight that residue sites 291, 292, 294, 295, 336, and 344 of CD26 are the crucial host range determinants for MjHKU4r-CoV-1. These results broaden our understanding of this potentially high-risk virus and will help us prepare for possible outbreaks in the future.
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