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Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Open accessAbstract
The recent emergence of a novel coronavirus (SARS-CoV-2) in China has caused significant public health concerns. Recently, ACE2 was reported as an entry receptor for SARS-CoV-2. In this study, we present the crystal structure of the C-terminal domain of SARS-CoV-2 (SARS-CoV-2-CTD) spike (S) protein in complex with human ACE2 (hACE2), which reveals a hACE2-binding mode similar overall to that observed for SARS-CoV. However, atomic details at the binding interface demonstrate that key residue substitutions in SARS-CoV-2-CTD slightly strengthen the interaction and lead to higher affinity for receptor binding than SARS-RBD. Additionally, a panel of murine monoclonal antibodies (mAbs) and polyclonal antibodies (pAbs) against SARS-CoV-S1/receptor-binding domain (RBD) were unable to interact with the SARS-CoV-2 S protein, indicating notable differences in antigenicity between SARS-CoV and SARS-CoV-2. These findings shed light on the viral pathogenesis and provide important structural information regarding development of therapeutic countermeasures against the emerging virus.
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“Attachment and entry of SARS-CoV-2 to target cells is initiated when the virus engages its cognate receptor, angiotensin-converting enzyme 2 (ACE2) via the receptor-binding domain (RBD) of the viral Spike protein, also called the S protein37.”
From SARS-CoV-2, COVID-19 and the aging immune system (2021) · cites this paper as [37]
In the citing paper
“The S2 subunit comprises the fusion peptide (FP), double heptad repeat (HR), central helix region (CH), connector domain (CD), transmembrane domain (TMD), and cytoplasmic tail (CT), and the S2 subunit is responsible for mediating the fusion between the virus and the host cell membrane233–236”
From Advances in COVID-19 mRNA vaccine development (2022) · cites this paper as [233]
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Self-citationDipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC
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InfluentialIsolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
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InfluentialSelf-citationA Novel Coronavirus Genome Identified in a Cluster of Pneumonia Cases — Wuhan, China 2019−2020
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InfluentialBat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond
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A distinct name is needed for the new coronavirus
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Self-citationEvaluation of candidate vaccine approaches for MERS-CoV
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MERS-CoV spike protein: Targets for vaccines and therapeutics
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Self-citationRecently Discovered Human Coronaviruses
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“Both alphaCoVs and the betaCoVs HCoV-OC43 and HKU1 cause self-limiting common cold-like illnesses (Chiu et al., 2005; Gorse et al., 2009; Jean et al., 2013; Jev snik et al., 2012).”
A human SARS-CoV neutralizing antibody against epitope on S2 protein
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SARS-like virus in the Middle East: A truly bat-related coronavirus causing human diseases
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Coronavirus infections in hospitalized pediatric patients with acute respiratory tract disease
Virant, M. J., Uršič, T., Žigon, N., Lusa, L., Krivec, U., & Petrovec, M. (2012) · BMC Infectious Diseases · doi:10.1186/1471-2334-12-365 · Cited by 62
Mouse Hepatitis Virus Receptor as a Determinant of the Mouse Susceptibility to MHV Infection
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InfluentialStructure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein
Han, X., Qi, J., Song, H., Wang, Q., Zhang, Y., Wu, Y., Lu, G., Yuen, K., Shi, Y., & Gao, G. F. (2017) · Virology · doi:10.1016/j.virol.2017.04.016 · Cited by 18 · cited 1×
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Self-citationZhang, X., Wang, J., Wen, K., Mou, Z., Zou, L., Che, X., Ni, B., & Wu, Y. (2009) · Viral Immunology · doi:10.1089/vim.2009.0046 · Cited by 12 · cited 4×
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Extrapulmonary manifestations of COVID-19
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Self-citation
Metadata
- Authors
- Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., Wang, Q., Zhou, H., Yan, J., & Qi, J.
- Affiliations
- Chinese Academy of Sciences (CN)
- Shanxi Agricultural University (CN)
- Anhui University (CN)
- Sichuan University (CN)
- University of Science and Technology of China (CN)
- University of Hong Kong (HK)
- Corresponding author
- Yan, Jinghua
- Qi, Jianxun
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-05
- Volume
- 181
- Issue
- 4
- Pages
- 894-904.e9
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7144619
- OpenAlex
- W3015190630
- Cited by
- 2,892
- References
- 59
- Citations by year
- 2026: 66 · 2025: 151 · 2024: 222 · 2023: 334 · 2022: 565 · 2021: 891 · 2020: 659
- FWCI
- 80.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Sichuan Province Science and Technology Support Program (2020YFS0010)
- Zhejiang University (2020XGZX031)
- West China Hospital, Sichuan University (HX-2019-nCoV-004)
- Chinese Academy of Sciences (XDB29010202, 2018119, XDB29040302)
- Sichuan University
- Youth Innovation Promotion Association of the Chinese Academy of Sciences
- Southern Medical University
- Ministry of Science and Technology of the People's Republic of China
- National Key Research and Development Program of China (2016YFD0500305)
- National Natural Science Foundation of China (81922044, 81973228, 81621091, 81673358)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- SARS-CoV-2, ACE2, viral entry receptor, spike protein, receptor binding domain, crystal structure, receptor binding affinity, SARS-CoV, antigenic differences, monoclonal antibodies, polyclonal antibodies
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, SARS-CoV-2, Amino Acid Sequence, Epitopes, Humans, Peptidyl-Dipeptidase A, Models, Molecular, Phylogeny, Sequence Alignment, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Spike Glycoprotein, Coronavirus
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