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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SARS-CoV-2 entry into target cells begins when the viral Spike protein receptor-binding domain engages ACE2.
“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]
The S2 subunit comprises FP, HR, CH, CD, TMD, CT, and is responsible for mediating fusion between virus and host cell membrane.
“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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InfluentialStructure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein
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“mAb1 and mAb2/mAb3 used in the above assay have been determined to bind to SARS-CoV S protein 330–350 and 380–399, respectively (Zhang et al., 2009).”
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Extrapulmonary manifestations of COVID-19
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Mechanisms of SARS-CoV-2 entry into cells
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The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
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“It is possible that antibodies in convalescent sera are able to neutralize these critical epitopes targeted by these mAbs that are known to disrupt the binding of the S protein to hACE2 receptor (Ju et al., 2020; Shi et al., 2020; Walls et al., 2020; Wang et al., 2020).”
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349 · see citing works
Self-citationSARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
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A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
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Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
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“Furthermore, while four RBD NAbs interacted with a stoichiometry of one Fab per trimer, consistent with one RBD being exposed in the “up state” and two in the less accessible “down state” ( 13, 40 ), COVA2-15 bound with a stoichiometry of three per trimer (Fig.”
BackgroundA human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286 · see citing works
Self-citationDistinct conformational states of SARS-CoV-2 spike protein
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221 · see citing works
Structures and distributions of SARS-CoV-2 spike proteins on intact virions
Ke, Z., Otón, J., Qu, K., Cortese, M., Žíla, V., McKeane, L., Nakane, T., Zivanov, J., Neufeldt, C. J., Cerikan, B., et al. (2020) · Nature · doi:10.1038/s41586-020-2665-2 · Cited by 1,114 · see citing works
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · see citing works
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19808-4 · Cited by 1,387 · see citing works
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060 · see citing works
“The S protein binds to the cellular surface receptor angiotensin-converting enzyme 2 (ACE2) through the receptor binding domain (RBD), an essential step for membrane fusion (Hoffmann et al., 2020; Lan et al., 2020; Shang et al., 2020; Wang et al., 2020; Yan et al., 2020; Zhou et al., 2020).”
Self-citationWu, Y., Wang, F., Shen, C., Peng, W., Li, D., Zhao, C., Li, Z., Li, S., Bi, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc2241 · Cited by 955 · see citing works
Self-citationCOVID-19: The first documented coronavirus pandemic in history
Liu, Y., Kuo, R.-L., & Shih, S. (2020) · Biomedical Journal · doi:10.1016/j.bj.2020.04.007 · Cited by 968 · see citing works
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SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development
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Human kidney is a target for novel severe acute respiratory syndrome coronavirus 2 infection
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De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
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“To assess the effect of noted RBD mutations on ACE2 binding, the crystal structure of the SARS-CoV-2 spike RBD domain complexed with ACE2 (PDB ID: 6LZG [15]) was used.”
MethodEmerging Pandemic Diseases: How We Got to COVID-19
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“, 2020), found on lung alveolar epithelial cells, gastrointestinal enterocytes, arterial and venous endothelial cells, and arterial smooth muscle cells, among other cell types (Hamming et al., 2004; Wang et al., 2020), which explains the excretion of SARS-CoV-2 and potential transmission via the respiratory and enteri…”
Antibody evasion by the P.1 strain of SARS-CoV-2
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“…pressure, as it mediates interaction with the cellular receptor and is also the site of binding for a major class of neutralizing antibodies that block the interaction of ACE2 with the RBD (Zost et al., 2020; Kreye et al., 2020; Wu et al., 2020; Yuan et al., 2020; Dejnirattisai et al., 2021).”
BackgroundUltrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
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The Natural History, Pathobiology, and Clinical Manifestations of SARS-CoV-2 Infections
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“Individuals taking immunosuppressive agents (Chen et al. 2020a), have hypertension, or have recently undergone surgeries are also at risk (Wang et al. 2020a).”
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“Until now, no effective drugs are clinically approved for these etiologic agents, but it appears that they share the same ACE2 receptor for entry into the host cells for reproduction and transmission [5,7,8].”
Toward Nanotechnology-Enabled Approaches against the COVID-19 Pandemic
Weiß, C., Carrière, M., Fusco, L., Capua, I., Regla-Nava, J. Á., Matteo Pasquali, A., Scott, J. A., Vitale, F., Ünal, M. A., Mattevi, C., et al. (2020) · ACS Nano · doi:10.1021/acsnano.0c03697 · Cited by 603 · see citing works
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SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity
Motozono, C., Toyoda, M., Zahradnik, J., Saito, A., Nasser, H., Tan, T. S., Ngare, I., Kimura, I., Uriu, K., Kosugi, Y., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.006 · Cited by 586 · see citing works
“Structural analyses have shown that the Y453 and N501 residues in the RBM are located at the interface between the SARS-CoV-2 RBM and human ACE2 and directly contribute to human ACE2 binding but that the L452 residue is not located at this interface (Lan et al., 2020;Wang et al., 2020; Zhao et al., 2020) (Figure 2A).”
Advances in COVID-19 mRNA vaccine development
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Geographic and Genomic Distribution of SARS-CoV-2 Mutations
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“This mutation causes a D614G (aspartate to glycine in protein position 614) aa-change of the Spike (S) protein, which is responsible for the initial entry of the virus in the cell via the ACE2 human receptor (Guzzi et al., 2020).”
BackgroundInfluentialStructural biology of SARS-CoV-2 and implications for therapeutic development
Yang, H.-T., & Rao, Z. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-021-00630-8 · Cited by 480 · see citing works
Both Boceprevir and GC376 efficaciously inhibit SARS-CoV-2 by targeting its main protease
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Self-citationRapid Generation of Neutralizing Antibody Responses in COVID-19 Patients
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“Recent studies have shown that the SARS-CoV-2 RBD interacts with the ACE2 receptor for cellular attachment.(5,6,10) Sequence analysis of the RBD shows extensive homology in this region to SARS (73%).”
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“3,55 SLC6A19, physiologically a neutral amino acid transporter, potentially can block the access of TMPRSS2 to ACE2 and subsequently reduce active infection.”
Broad neutralization of SARS-related viruses by human monoclonal antibodies
Wec, A. Z., Wrapp, D., Herbert, A. S., Maurer, D. P., Haslwanter, D., Sakharkar, M., Jangra, R. K., Dieterle, M. E., Lilov, A., Huang, D., et al. (2020) · Science · doi:10.1126/science.abc7424 · Cited by 520 · see citing works
“tigenic sites are rarely targeted by nAbs (5, 9, 12, 13).”
BackgroundBat coronaviruses related to SARS-CoV-2 and infectious for human cells
Temmam, S., Vongphayloth, K., Baquero, E., Munier, S., Bonomi, M., Regnault, B., Douangboubpha, B., Karami, Y., Chrétien, D., Sanamxay, D., et al. (2022) · Nature · doi:10.1038/s41586-022-04532-4 · Cited by 519 · see citing works
Recent Developments on Therapeutic and Diagnostic Approaches for COVID-19
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A Universal Design of Betacoronavirus Vaccines against COVID-19, MERS, and SARS
Dai, L., Zheng, T., Xu, K., Han, Y., Xu, L., Huang, E., An, Y., Cheng, Y., Li, S., Liu, M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.035 · Cited by 476 · see citing works
Self-citationReceptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
Han, P., Li, L., Liu, S., Wang, Q., Zhang, D., Xu, Z., Han, P., Li, X., Peng, Q., Su, C., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.001 · Cited by 491 · see citing works
“As previously reported (Wang et al., 2020), the binding interface of hACE2 for SARS-CoV-2 RBD is distributed over two patches.”
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Syncytia formation by SARS‐CoV‐2‐infected cells
Buchrieser, J., Dufloo, J., Hubert, M., Monel, B., Planas, D., Rajah, M. M., Planchais, C., Porrot, F., Guivel‐Benhassine, F., Van der Werf, S., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2020106267 · Cited by 462 · see citing works
“The structure of S in complex with ACE2 has been elucidated (Lan et al , 2020; Walls et al , 2020; Wang et al , 2020).”
An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike
Schoof, M., Faust, B., Saunders, R. A., Sangwan, S., Rezelj, V. V., Hoppe, N., Boone, M., Billesbølle, C. B., Puchades, C., Azumaya, C. M., et al. (2020) · Science · doi:10.1126/science.abe3255 · Cited by 428 · see citing works
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Self-citationSARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
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Severe covid-19 pneumonia: pathogenesis and clinical management
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Structural impact on SARS-CoV-2 spike protein by D614G substitution
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Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron
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“The entry for SARS-CoV-2 involves interactions of S with the ACE2 receptor and known or unidentified attachment cofactors, and subsequent priming of the protein by host cell proteases (Lan et al., 2020; Shang et al., 2020; Wang et al., 2020).”
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman‐Duhovny, D., Zhang, C., & Shi, Y. (2020) · Science · doi:10.1126/science.abe4747 · Cited by 394 · see citing works
The emergence, genomic diversity and global spread of SARS-CoV-2
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Are pangolins the intermediate host of the 2019 novel coronavirus (SARS-CoV-2)?
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“Structurally, RBD consists of two subdomains: a core and an external subdomain (51, 52).”
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Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape
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SARS-CoV-2, COVID-19 and the aging immune system
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ACE2, Much More Than Just a Receptor for SARS-COV-2
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“…— the crown-like spike (S) glycoprotein that binds to human ACE2 receptor to mediate the entry of the virus in the host cell (Walls et al , 2020; Wang et al , 2020), the membrane (M) protein that facilitates viral assembly in the endoplasmic reticulum, the ion channel envelope (E) protein,…”
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“The exact entry process for SARS-CoV-2 is still being defined but is known to involve spike interaction with the ACE2 receptor (Lan et al., 2020; Shang et al., 2020b; Wang et al., 2020; Zhou et al., 2020a).”
Impaired local intrinsic immunity to SARS-CoV-2 infection in severe COVID-19
Ziegler, C. G. K., Miao, V. N., Owings, A. H., Navia, A. W., Tang, Y., Bromley, J. D., Lotfy, P., Sloan, M., Laird, H., Williams, H. B., et al. (2021) · Cell · doi:10.1016/j.cell.2021.07.023 · Cited by 349 · see citing works
“…and viral shedding by asymptomatic or presymp- Cell 184, 1–21, Se This is an open access article und tomatic individuals contributes to enhanced transmissibility (Fears et al., 2020; Meyerowitz et al., 2021) and rapid community spread (Arons et al., 2020; Sakurai et al., 2020; Wang et al., 2020c).”
Structural insights into SARS-CoV-2 proteins
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“SARS-CoV-2 S protein shares ~77% sequence identity with SARS-CoV S protein, and binds to the human ACE2 receptor for virion’s entry into the host cells.(120,121) The 1273 residues long S protein has two major subunits, S1 and S2 (Fig.”
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An alpaca nanobody neutralizes SARS-CoV-2 by blocking receptor interaction
Hanke, L., Vidakovics, L. P., Sheward, D. J., Das, H., Schulte, T. P., Moliner-Morro, A., Corcoran, M., Achour, A., Hedestam, G. B. K., Hällberg, B. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18174-5 · Cited by 327 · see citing works
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“Rapid human‐to‐human transmission is the most striking feature of SARS‐CoV‐2, which enabled its worldwide penetrations (Wang et al., 2020b).”
BackgroundResultInfluentialOudkerk, M., Buller, H. R., Kuijpers, D., van Es, N., Oudkerk, S. F., McLoud, T. C., Gommers, D. A. M. P. J., van Dissel, J., Cate, H. T., & van Beek, E. J. R. (2020) · Radiology · doi:10.1148/radiol.2020201629 · Cited by 345 · see citing works
“SARS-CoV-2 enters cells by endocytosis after binding to the transmembrane angiotensin converting enzyme-2 (ACE2) protein on cells in the lung, heart, blood vessels, kidney, and gastrointestinal tract (2).”
BackgroundMolecular mechanism of interaction between SARS-CoV-2 and host cells and interventional therapy
Zhang, Q., Xiang, R., Huo, S., Zhou, Y., Jiang, S., Wang, Q., & Yu, F. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00653-w · Cited by 341 · see citing works
Self-citationNeutralization of SARS-CoV-2 by Destruction of the Prefusion Spike
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Erratum To: Syncytia formation by SARS‐CoV‐2‐infected cells
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Skin Aging, Cellular Senescence and Natural Polyphenols
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Towards effective COVID‑19 vaccines: Updates, perspectives and challenges (Review)
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“In the case of SARS-cOV-2, the receptor is the angiotensin converting enzyme 2 (AcE2), which is found in large quantities in the respiratory tract and lung parenchyma (51-54).”
BackgroundWang, Y., Liu, M., & Gao, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008209117 · Cited by 305 · see citing works
“Curiously, a SARS-CoV neutralizing antibody, 80R, that recognizes the S protein with nanomolar affinity (14) in the same interfacial region of ACE2 does not show detectable binding to the RBD of SARS-CoV-2 (11, 15).”
BackgroundMethodInfluentialACE2: Evidence of role as entry receptor for SARS-CoV-2 and implications in comorbidities
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SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
Coinfection with influenza A virus enhances SARS-CoV-2 infectivity
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Self-citationAn aberrant STAT pathway is central to COVID-19
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COVID-19 pandemic: Insights into structure, function, and hACE2 receptor recognition by SARS-CoV-2
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“The equilibrium dissociation constants (KD) for hACE2 interacting with the S proteins have indicated that the binding affinity of SARS-CoV-2-S is several-fold higher than that of SARSCoV [11,17,69].”
BackgroundInfluentialTreatment of Coronavirus Disease 2019 (COVID-19) Patients with Convalescent Plasma
Salazar, E., Perez, K. K., Ashraf, M., Chen, J., Castillo, B., Christensen, P. A., Eubank, T. A., Bernard, D. W., Eagar, T. N., Long, S. W., et al. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.05.014 · Cited by 294 · see citing works
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Tan, T. K., Rijal, P., Rahikainen, R., Keeble, A. H., Schimanski, L. M., Hussain, S., Harvey, R., Hayes, J. W. P., Edwards, J. C., McLean, R. K., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20654-7 · Cited by 285 · see citing works
Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody
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Does the human placenta express the canonical cell entry mediators for SARS-CoV-2?
Piqué-Regi, R., Romero, R. J., Tarca, A. L., Luca, F., Xu, Y., Alazizi, A., Leng, Y., Hsu, C., & Gomez‐Lopez, N. (2020) · eLife · doi:10.7554/elife.58716 · Cited by 280 · see citing works
“Cell entry and spreading of SARS-CoV-2 has been widely thought to depend on the angiotensinconverting enzyme 2 (ACE2) receptor [57, 58] and the serine protease TMPRSS2 [59].”
BackgroundThree-dimensional human alveolar stem cell culture models reveal infection response to SARS-CoV-2
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“Essential features of SARS-CoV-2 virus, including ACE2 dependency for cellular entry, patterns of viral transcription, and structure of the spike protein, have been identified (Hoffmann et al., 2020; Kim et al., 2020a; Walls et al., 2020; Wang et al., 2020).”
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“…et al., 2020; Gordon et al., 2020; Ko et al., 2020; Wang et al., 2020a, 2020b; Wit et al., 2020), tocilizumab, corticosteroids (Loutfy et al., 2003; Smith et al., 2020), certain nucleotide as inhibitors (Elfiky, 2020), COVID-19 protease inhibitors (Liu and Wang, 2020, Table 1) are few to name them.”
SARS-CoV-2 escape <i>in vitro</i> from a highly neutralizing COVID-19 convalescent plasma
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“The S1 subunit presents two highly immunogenic domains, the N-terminal domain (NTD) and the RBD, which are the major targets of polyclonal and monoclonal neutralizing antibodies (4, 9, 10).”
A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein
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COVID-19: A review of therapeutic strategies and vaccine candidates
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Engineered ACE2 receptor traps potently neutralize SARS-CoV-2
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“High-resolution ACE2–RBD structures (22, 23) show a large, flat binding interface primarily comprising the N-terminal helices of ACE2 (residues 18 to 90), with secondary interaction sites spanning residues 324 to 361 (Fig.”
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“Specifically, the regions, Leu455 to Pro491 and Asn501 to Val503 show disorder-to-order transitions [61].”
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Neurological manifestations of long-COVID syndrome: a narrative review
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- 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 · 2019: 1 · 2013: 1
- 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
- Physical Sciences › Materials Science › Materials Chemistry › 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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