The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
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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“After the outbreak of COVID-19, Chinese scientists promptly determined that SARSCoV-2 also utilizes hACE2 for cell entry (Zhou et al., 2020).”
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“As of February 24, 2020, 79,331 laboratory-confirmed cases have been reported to the WHO globally, with 77,262 cases in China, including 2,595 deaths (https://www.who.int/).”
BackgroundInfluentialSelf-citationCryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897 · cited 4×
“Notably, two cryo-EM structures of trimeric SARS-CoV-2 S proteins were also published recently, with the receptor binding region buried or exposed (Walls et al., 2020; Wrapp et al., 2020), which is consistent with the structural features of MERS-CoV and SARS-CoV S proteins (Yuan et al.”
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“Later, the International Committee on Taxonomy of Viruses (ICTV) officially designated the virus SARS-CoV-2 (Coronaviridae Study Group of the International Committee on Taxonomy of Viruses, 2020), although many virologists argue that HCoV-19 is more appropriate (Jiang et al., 2020).”
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Extrapulmonary manifestations of COVID-19
Gupta, A., Madhavan, M. V., Sehgal, K., Nair, N., Mahajan, S., Sehrawat, T. S., Bikdeli, B., Ahluwalia, N., Ausiello, J. C., Wan, E. Y., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0968-3 · Cited by 3,185
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022
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SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
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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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