Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2
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Abstract
There is an urgent need for animal models to study SARS-CoV-2 pathogenicity. Here, we generate and characterize a novel mouse-adapted SARS-CoV-2 strain, MASCp36, that causes severe respiratory symptoms, and mortality. Our model exhibits age- and gender-related mortality akin to severe COVID-19. Deep sequencing identified three amino acid substitutions, N501Y, Q493H, and K417N, at the receptor binding domain (RBD) of MASCp36, during in vivo passaging. All three RBD mutations significantly enhance binding affinity to its endogenous receptor, ACE2. Cryo-electron microscopy analysis of human ACE2 (hACE2), or mouse ACE2 (mACE2), in complex with the RBD of MASCp36, at 3.1 to 3.7 Å resolution, reveals the molecular basis for the receptor-binding switch. N501Y and Q493H enhance the binding affinity to hACE2, whereas triple mutations at N501Y/Q493H/K417N decrease affinity and reduce infectivity of MASCp36. Our study provides a platform for studying SARS-CoV-2 pathogenesis, and unveils the molecular mechanism for its rapid adaptation and evolution.
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The Omicron spike harbors mutations Q493R and Q498R, which are related to exchanges Q493K and Q498H detected in mouse-adapted SARS-CoV-2.
“In addition, the Omicron spike harbors mutations Q493R and Q498R, which are related to exchanges Q493K and Q498H, which were also detected in mouse-adapted SARS-CoV-2”
From The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic (2022) · cites this paper as Sun et al., 2021
Efficient usage of murine ACE2 by the Omicron spike is in keeping with the presence of mutations K417N and N501Y, which can emerge upon SARS-CoV-2 adaptation to experimentally infected mice.
“The efficient usage of murine ACE2 is in keeping with the presence of the mutations K417N and N501Y, which can also emerge upon SARS-CoV-2 adaptation to experimentally infected mice”
From The Omicron variant is highly resistant against antibody-mediated neutralization: Implications for control of the COVID-19 pandemic (2022) · cites this paper as Sun et al., 2021
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- Authors
- Sun, S., Gu, H., Cao, L., Chen, Q., Ye, Q., Yang, G., Li, R.-T., Fan, H., Deng, Y.-Q., Song, X., Qi, Y., Li, M., Lan, J., Feng, R., Guo, Y., Zhu, N., Qin, S., Wang, L., Zhang, Y.-F., Zhou, C., Zhao, L., Chen, Y., Shen, M., Cui, Y., Yang, X., Wang, X., Tan, W., Wang, H., Wang, X., & Qin, C.-F.
- Affiliations
- Beijing Institute of Microbiology and Epidemiology (CN)
- Chinese Academy of Sciences (CN)
- Beijing Proteome Research Center (CN)
- Chinese Center For Disease Control and Prevention (CN)
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- Corresponding author
- Wang, Xinquan
- Qin, Cheng-Feng
- ORCID
- Venue
- Nature Communications
- Published
- 2021-09-27
- Volume
- 12
- Issue
- 1
- Pages
- 5654-5654
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC8476561
- OpenAlex
- W3202702853
- Cited by
- 104
- References
- 62
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 14 · 2023: 11 · 2022: 42 · 2021: 26
- FWCI
- 7.36
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Science Foundation of China | Young Scientists Fund (81925025)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Keywords
- SARS-CoV-2, mouse-adapted virus, animal model of COVID-19, receptor-binding domain mutations, N501Y, K417N, ACE2, receptor binding affinity, viral adaptation, viral evolution, mouse mortality, respiratory diseases
- MeSH terms
- Protein Domains, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Animals, Binding Sites, Disease Models, Animal, Female, Humans, Male, Protein Binding, Severity of Illness Index, Amino Acid Substitution, Mice, Spike Glycoprotein, Coronavirus
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