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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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“After the outbreak of COVID-19, Chinese scientists promptly determined that SARSCoV-2 also utilizes hACE2 for cell entry (Zhou et al., 2020).”
InfluentialHoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286
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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.”
BackgroundResultInfluentialGorbalenya, A. E., Baker, S. C., Baric, R. S., de Groot, R. J., Drosten, C., Gulyaeva, A. A., Haagmans, B. L., Lauber, C., Leontovich, A. M., Neuman, B. W., et al. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0695-z · Cited by 8,745 · cited 1×
“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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Adverse Cardiovascular Effects of Anti-COVID-19 Drugs
Liu, D., Zeng, X., Ding, Z., Lv, F., Mehta, J. L., & Wang, X. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.699949 · Cited by 29
A perspective on the applications of furin inhibitors for the treatment of SARS-CoV-2
Devi, K. P., Pourkarim, M. R., Thijssen, M., Sureda, A., Khayatkashani, M., Cismaru, C. A., Neagoe, I. B., Habtemariam, S., Razmjouei, S., & Kashani, H. R. K. (2022) · Pharmacological Reports · doi:10.1007/s43440-021-00344-x · Cited by 30
“Subunit S1 contains the receptor binding domain that binds ACE2 on the host cells [8].”
BackgroundSARS-CoV-2 Susceptibility and ACE2 Gene Variations Within Diverse Ethnic Backgrounds
Vadgama, N., Kreymerman, A., Campbell, J. A., Shamardina, O., Brugger, C., Deaconescu, A. M., Lee, R. T., Penkett, C. J., Gifford, C. A., Mercola, M. A., et al. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.888025 · Cited by 31
Essa, R. Z., Wu, Y. S., Batumalaie, K., Sekar, M., & Poh, C. L. (2022) · Pharmacological Reports · doi:10.1007/s43440-022-00432-6 · Cited by 29
“Next, HD5 peptide is a peptide secreted by Paneth cells in the crypts of Lieberkühn that has a high affinity toward ACE2 receptors [74].”
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“Recently, it has been reported that the interactions between the Sprotein RBD of SARS-CoV-2 and the human ACE2 receptor (Turoňová et al., 2020; Wang et al., 2020) could provide important targets for candidate screening and identification by inhibiting the entry of the viral particle into humans,…”
BackgroundBadhe, Y. P., Gupta, R., & Rai, B. (2021) · RSC Advances · doi:10.1039/d0ra09123e · Cited by 30
SARS‐CoV‐2 immunogenicity at the crossroads
Karamloo, F., & König, R. (2020) · Allergy · doi:10.1111/all.14360 · Cited by 28
“S binds to human ACE2 with higher affinity than the SARS-CoV S protein, 3,4 which may impact viral infectivity for SARS-CoV-2.”
BackgroundLack of antibody-mediated cross-protection between SARS-CoV-2 and SARS-CoV infections
Yang, R., Lan, J., Huang, B., Ruhan, A., Lu, M., Wang, W., Wang, W., Li, W., Deng, Y. L., Wong, G., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102890 · Cited by 28
Structural basis for the multimerization of nonstructural protein nsp9 from SARS-CoV-2
Zhang, C., Chen, Y., Li, L., Yang, Y., He, J., Chen, C., & Su, D. (2020) · Molecular Biomedicine · doi:10.1186/s43556-020-00005-0 · Cited by 28
“The life cycle of SARS-CoVs starts with its binding to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) through its spike glycoproteins, resulting in receptor-mediated endocytosis [10].”
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“…receptor, proteolitic cleavage followed by conformational change thought to assist viral entry (Kam et al., 2009), local dehydration and ordering of the membrane upon interaction with the fusion peptide (Lai et al., 2017), and culminating with membrane fusion and virus entry (Wang et al., 2020b).”
In silico identification of strong binders of the SARS-CoV-2 receptor-binding domain
Behloul, N., Baha, S., Guo, Y., Yang, Z., Shi, R., & Meng, J. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173701 · Cited by 28
“…with the arch-shaped α1 helix of the ACE2 and to a minor extent with the α2 helix and the loop connecting the β3 and β4 antiparallel strands of ACE2 (Yan et al., 2020); the residues of the RBD playing a pivotal role in the interaction have been identified (Wang et al., 2020; Yan et al., 2020).”
BackgroundInfluentialAl-Sehemi, A. G., Olotu, F. A., Dev, S., Pannipara, M., Soliman, M. E. S., Carradori, S., & Mathew, B. (2020) · ChemistrySelect · doi:10.1002/slct.202003349 · Cited by 28
COVID-19: The Emerging Immunopathological Determinants for Recovery or Death
Ahmad, T., Chaudhuri, R., Joshi, M. C., Almatroudi, A., Rahmani, A. H., & Ali, S. M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.588409 · Cited by 30
Islam, M. T., Alam, A. S. M. R. U., Sakib, N., Hasan, M. S., Chakrovarty, T., Tawyabur, M., Islam, O. K., Al‐Emran, H. M., Jahid, M. I. K., & Hossain, M. A. (2021) · Journal of Medical Virology · doi:10.1002/jmv.26818 · Cited by 28
Gadanec, L. K., Qaradakhi, T., McSweeney, K. R., Ali, B. A., Zulli, A., & Apostolopoulos, V. (2021) · Future Microbiology · doi:10.2217/fmb-2021-0018 · Cited by 29
Li, M., Guo, J., Lu, S., Zhou, R., Shi, H., Shi, X., Cheng, L., Liang, Q., Liu, H., Wang, P., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.697074 · Cited by 25
“At the initial outbreak of SARS-CoV-2, we and others resolved the crystal structure of the SARS-CoV-2 RBD bound to ACE2, which revealed that the overall ACE2binding mode is nearly identical to that of the SARS-CoV RBD (20, 26–28).”
BackgroundSelf-citationIdentifying Primate ACE2 Variants That Confer Resistance to SARS-CoV-2
Bhattacharjee, M. J., Lin, J.-J., Chang, C.-Y., Chiou, Y.-T., Li, T., Tai, C.-W., Shiu, T.-F., Chen, C., Chou, C.-Y., Chakraborty, P., et al. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab060 · Cited by 28
Nayak, K., Gottimukkala, K. P., Kumar, S., Reddy, E. S., Edara, V. V., Kauffman, R. C., Floyd, K. A., Mantus, G. E., Savargaonkar, D., Goel, P. K., et al. (2021) · Virology · doi:10.1016/j.virol.2021.02.002 · Cited by 28
“Moreover, given that many of the SARS-CoV-2 neutralizing epitopes are located in the viral 95 receptor binding domain (RBD) of the Spike (S) protein (21-29), it is important to evaluate 96 the relationship between RBD-specific IgG titers and neutralizing antibody responses.”
BackgroundA study on non-synonymous mutational patterns in structural proteins of SARS-CoV-2
Das, J. K., & Roy, S. (2021) · Genome · doi:10.1139/gen-2020-0157 · Cited by 28
Clinical course and outcome among patients with acute pancreatitis and COVID-19
Kumar, V., Barkoudah, E., de Souza, D. A. T., Jin, D. X., & McNabb-Baltar, J. Y. (2021) · European Journal of Gastroenterology & Hepatology · doi:10.1097/meg.0000000000002160 · Cited by 28
IgM and IgG Immunoreactivity of SARS-CoV-2 Recombinant M Protein
Lopandić, Z., Protić-Rosić, I., Todorović, A., Glamočlija, S., Gnjatović, M., Ćujić, D., & Gavrović-Jankulović, M. Đ. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094951 · Cited by 30
“The wide range of clinical manifestations is probably due to the virus infecting almost every human cell [6].”
BackgroundNanobased Platforms for Diagnosis and Treatment of COVID-19: From Benchtop to Bedside
Bidram, E., Esmaeili, Y., Amini, A., Sartorius, R., Tay, F. R., Shariati, L., & Makvandi, P. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.1c00318 · Cited by 27
Zhang, Y., He, X., Zhai, J., Ji, B., Man, V. H., & Wang, J. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab188 · Cited by 27
“Just like SARSCoV, SARS-CoV-2 infects host cells utilizing hACE2 expressed by HeLa cells as the receptor, [22] and the spike-hACE2 binding triggers a cascade of immune reactions.”
BackgroundSelf-citationFernandez, R. A. T., Quimque, M. T. J., Notarte, K. I., Manzano, J. A., Pilapil, D. Y. H., de Leon, V. N., Jose, J. J. P. S., Villalobos, O. A., Muralidharan, N. H., Gromiha, M. M., et al. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1969281 · Cited by 29
“Key residue substitutions in the C-terminal domain of the S protein strengthen interaction with ACE2 leading to higher binding affinity (Wang et al., 2020).”
BackgroundArooj, M., Shehadi, I. A., Nassab, C. N., & Mohamed, A. A. M. (2021) · Chemical Papers · doi:10.1007/s11696-021-01843-0 · Cited by 28
Showers, W. M., Leach, S. M., Kechris, K. J., & Strong, M. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.105153 · Cited by 35
Yuan, T. Z., Garg, P., Wang, L., Willis, J. R., Kwan, E., Hernandez, A. G. L., Tuscano, E., Sever, E. N., Rivera, E. K., Soto, C. S., et al. (2021) · mAbs · doi:10.1080/19420862.2021.2002236 · Cited by 31
“Similar to SARS-CoV, SARS-CoV -2 uses the trimeric spike (S) to enable cell entry.(9,10) These glycoproteins are made up of two subunits (S1 and S2) and decorate the surface of the virion.”
MethodPlastic Antibodies Mimicking the ACE2 Receptor for Selective Binding of SARS‐CoV‐2 Spike
Batista, A. D., Rajpal, S., Keitel, B., Dietl, S., Fresco‐Cala, B., Dinc, M., Groß, R. M., Sobek, H., Münch, J., & Mizaikoff, B. (2022) · Advanced Materials Interfaces · doi:10.1002/admi.202101925 · Cited by 27
Known Cellular and Receptor Interactions of Animal and Human Coronaviruses: A Review
Everest, H., Stevenson-Leggett, P., Bailey, D., Bickerton, E., & Keep, S. (2022) · Viruses · doi:10.3390/v14020351 · Cited by 28
Gao, J., Mei, H., Sun, J., Li, H., Huang, Y., Tang, Y., Duan, L., Liu, D., Pang, Y., Wang, Q., et al. (2022) · Advanced Biology · doi:10.1002/adbi.202200007 · Cited by 28
Self-citationVardhan, S., & Sahoo, S. K. (2022) · Comput. Biol. Medicine · doi:10.1016/j.compbiomed.2022.105367 · Cited by 30
Scheim, D. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052558 · Cited by 32
“Viruses fuse and then replicate via host cell receptors specific to the viral strain, which is ACE2 for SARS-CoV-2 [23,24].”
BackgroundPhotodynamic disinfection of SARS-CoV-2 clinical samples using a methylene blue formulation
Lobo, C. S., Rodrigues‐Santos, P., Pereira, D., Núñez, J. G., Trêpa, J., Sousa, D. L., Lourenço, J. V., Coelho, M. F., de Almeida, L. P., da Cunha, J. S., et al. (2022) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-022-00202-6 · Cited by 28
“Pseudotyped lentiviral vectors (LVs) encoding luciferase were produced in HEK293T cells, as previously described [35], with slightly modifications, using polyethylenimine (PEI) [36].”
MethodRecent advances in small-molecular therapeutics for COVID-19
Zhong, L., Zhao, Z., Peng, X., Zou, J., & Yang, S. (2022) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbac024 · Cited by 29
Abeywardhana, S., Premathilaka, M. B., Bandaranayake, U., Perera, D., & Peiris, L. (2022) · Journal of Medical Virology · doi:10.1002/jmv.28406 · Cited by 24
“We observed the formation of a salt bridge between K417 (RBD) and D38 (hACE‐2) in the WT RBD‐hACE2 complex confirming the results obtained by Wang et al.(33) However, the K417 was substituted by N417 and T417, respectively, in Beta and Gamma, resulting in the loss of the salt bridge.”
ResultReuter, N., Chen, X., Kropff, B., Peter, A. S., Britt, W. J., Mach, M., Überla, K., & Thomas, M. (2023) · Viruses · doi:10.3390/v15071500 · Cited by 30
“The S1 subunit harboring the receptor-binding domain (RBD) binds to the host angiotensin-converting enzyme 2 (ACE2) [10,11].”
BackgroundChowdhury, R., & Maranas, C. D. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.30.015891 · Cited by 28
Bromelain Inhibits SARS-CoV-2 Infection in VeroE6 CellsPreprint
Sagar, S., Ashokkumar, R., Lutz, W. E., Struble, L. R., Khurana, S., Schnaubelt, A. T., Mishra, N. K., Guda, C., Broadhurst, M. J., Reid, S. P., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.16.297366 · Cited by 28
“It has several functional domains, including N-terminal domain (NTD), receptor-binding domain (RBD), fusion peptide (FP), heptad repeat 1(HR1), central helix (CH), connector domain (CD), transmembrane domain (TM), and a cytoplasmic tail (CT) (11).”
SARS-CoV-2 mutations in Brazil: from genomics to putative clinical conditions
Timmers, L. F. S. M., Peixoto, J. V., Ducati, R. G., Bachega, J. F. R., Pereira, L. D. M., Caceres, R. A., Majolo, F., da Silva, G. L., Anton, D. B., Dellagostin, O. A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-91585-6 · Cited by 30
Structural basis of SARS-CoV-2 spike protein induced by ACE2
Meirson, T., Bomze, D., & Markel, G. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa744 · Cited by 27
An Early Pandemic Analysis of SARS-CoV-2 Population Structure and Dynamics in Arizona
Ladner, J. T., Larsen, B. B., Bowers, J. R., Hepp, C. M., Bolyen, E. K., Folkerts, M., Sheridan, K. L., Pfeiffer, A., Yaglom, H. D., Lemmer, D., et al. (2020) · mBio · doi:10.1128/mbio.02107-20 · Cited by 27
“Structural studies indicate that A475 interacts with S19 of ACE2 (24, 25).”
Chauhan, N., Soni, S., Gupta, A., Aslam, M., & Jain, U. (2020) · Journal of Medical Virology · doi:10.1002/jmv.26709 · Cited by 26
Huang, S., Miller, S. O., Yen, C., & Wang, S. (2020) · Genes · doi:10.3390/genes12010016 · Cited by 27
“The SARS-CoV-2 receptor-binding domain (RBD) located in the S1 domain binds to the host cell ACE2 receptor, while S2 functions as the membrane fusion subunit [15,16].”
BackgroundNg, K. T., Mohd-Ismail, N. K., & Tan, Y. (2021) · Vaccines · doi:10.3390/vaccines9020178 · Cited by 28
Luo, Y. R., Yun, C., Chakraborty, I., Wu, A. H. B., & Lynch, K. L. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00193-21 · Cited by 24
“Although the RBD-ACE2 interaction mainly characterizes viral attachment (17,23), it mimics the virus-host cell interaction since viral attachment is the main determinate of viral entry into host cells.”
BackgroundSARS-CoV-2 cell entry and targeted antiviral development
Chen, Z., Du, R., Achi, J. G., Rong, L., & Cui, Q. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.05.007 · Cited by 27
“To better understand the receptor recognition mechanism, crystal structure of the RBDbound to ACE2 was determined 20 e 23 .”
Wang, Q., Wang, L., Zhang, Y., Zhang, X., Zhang, L., Shang, W., & Bai, F. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00320 · Cited by 25
Self-citationAzimirad, M., Noori, M., Raeisi, H., Yadegar, A., Shahrokh, S., Aghdaei, H. A., Bentivegna, E., Martelletti, P., Petrosillo, N., & Zali, M. R. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.775063 · Cited by 31
“Studies have shown that ACE2 is the target of SARS-CoV-2 (27, 120) which is highly expressed in colonocytes of patients with inflammatory bowel disease and can regulate amino acid transport, microbial ecology, and inflammation in the gut and create conditions favorable for coronaviruses infection (11, 120).”
BackgroundComputational Study of SARS-CoV-2 RNA Dependent RNA Polymerase Allosteric Site Inhibition
Faisal, S., Badshah, S. L., Kubra, B., Sharaf, M., Emwas, A.-H. M., Jaremko, M., & Abdalla, M. (2021) · Molecules · doi:10.3390/molecules27010223 · Cited by 27
“Cellular entry of SARS-CoV-2 is mediated by the interaction of the virus S-protein and the host hACE-2 receptor [14,15].”
BackgroundControl of SARS-CoV-2 infection by MT1-MMP-mediated shedding of ACE2
Guo, X., Cao, J., Cai, J.-P., Wu, J., Huang, J., Asthana, P., Wong, S. K. K., Ye, Z.-W., Gurung, S., Zhang, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35590-x · Cited by 25
Self-citationPotential of Lactoferrin in the Treatment of Lung Diseases
Kaczyńska, K., Jampolska, M., Wojciechowski, P., Sulejczak, D., Andrzejewski, K., & Zając, D. (2023) · Pharmaceuticals · doi:10.3390/ph16020192 · Cited by 28
“The SARS-CoV-2 spike protein binds to heparan sulfate proteoglycans, attaching the virus to the surface of the target cell and interacts with the angiotensin-converting enzyme 2 receptor (ACE2), allowing the virus to enter the cell [94,95].”
BackgroundMatino, E., Tavella, E., Rizzi, M., Avanzi, G. C., Azzolina, D., Battaglia, A., Becco, P., Bellan, M., Bertinieri, G., Bertoletti, M., et al. (2023) · Nutrients · doi:10.3390/nu15051285 · Cited by 27
Hsu, A., Wang, G., Reid, A. T., Veerati, P. C., Pathinayake, P. S., Daly, K., Mayall, J., Hansbro, P. M., Horvat, J. C., Wang, F., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.317818 · Cited by 27
“SARS-CoV-2 belongs to the beta-coronavirus genus with approximately 79.5% sequence homology to the SARS-CoV that emerged in 2002 (Wang et al., 2020b).”
BackgroundInfluentialCheng, F., Rao, S., & Mehra, R. (2020) · Cleveland Clinic Journal of Medicine · doi:10.3949/ccjm.87a.ccc037 · Cited by 26
“Our hypothesis is based on the following: (1) the proteins that functionally associate with viral infection are localized in the corresponding subnetwork within the comprehensive human PPI network; and (2) the proteins that serve as drug targets for a specific disease may also be suitable drug targets for potential an…”
Mallis, P., Michalopoulos, Ε., Chatzistamatiou, T. K., & Stavropoulos‐Giokas, C. (2020) · World Journal of Stem Cells · doi:10.4252/wjsc.v12.i8.731 · Cited by 26
Severe Acute Respiratory Distress Syndrome Secondary to Coronavirus 2 (SARS-CoV-2)
Maveddat, A., Mallah, H., Rao, S., Ali, K., Sherali, S., & NUGENT, K. M. (2020) · The International Journal of Occupational and Environmental Medicine · doi:10.34172/ijoem.2020.2202 · Cited by 26
“com Vol 11, Num 4; October, 2020 159 says, demonstrating a 4-fold higher affinity of SARS-CoV-2 to human ACE2 in comparison to SARS-CoV.(6) Genome sequencing of SARS-CoV-2 compared to other human and animal virus genomes demonstrates a close relation to the several other viruses, including bat-SL-CoV2XC21 and bat-SL-C…”
BackgroundResultBarre, A., Damme, E. J. M. V., Simplicien, M., Benoist, H., & Rougé, P. (2020) · Marine Drugs · doi:10.3390/md18110543 · Cited by 27
Cameron, A., Porterfield, C. A., Byron, L. D., Wang, J., Pearson, Z., Bohrhunter, J. L., Cardillo, A. B., Ryan-Muntz, L., Sorensen, R. A., Caserta, M. T., et al. (2020) · Journal of Clinical Microbiology · doi:10.1128/jcm.02489-20 · Cited by 27
Potential Therapeutic Effect of Traditional Chinese Medicine on Coronavirus Disease 2019: A Review
Qiu, Q., Huang, Y., Liu, X., Huang, F., Li, X., Cui, L., Luo, H., & Luo, L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.570893 · Cited by 26
Drawing Comparisons between SARS-CoV-2 and the Animal Coronaviruses
Ghosh, S., & Malik, Y. S. (2020) · Microorganisms · doi:10.3390/microorganisms8111840 · Cited by 28
Nunes-Santos, C. J., Kuehn, H. S., & Rosenzweig, S. D. (2020) · Journal of Clinical Immunology · doi:10.1007/s10875-020-00905-4 · Cited by 26
Admin, A., Batchu, S. N., Kaur, H., Yerra, V. G., Advani, S. L., Kabir, G., Liu, Y., Klein, T., & Advani, A. (2020) · Diabetes · doi:10.2337/db20-0765 · Cited by 26
Molecular-Level Anatomy of SARS-CoV-2 for the Battle against the COVID-19 Pandemic
Komiyama, M. (2021) · Bulletin of the Chemical Society of Japan · doi:10.1246/bcsj.20210030 · Cited by 27
Kalra, R. S., Kumar, V., Dhanjal, J. K., Garg, S., Li, X., Kaul, S. C., Sundar, D., & Wadhwa, R. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1902858 · Cited by 26
Comparative Analysis of Antigen-Specific Anti–SARS-CoV-2 Antibody Isotypes in COVID-19 Patients
Fujigaki, H., Inaba, M., Osawa, M., Moriyama, S., Takahashi, Y., Suzuki, T., Yamase, K., Yoshida, Y., Yagura, Y., Oyamada, T., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001369 · Cited by 27
Kalashnyk, O., Lykhmus, O., Izmailov, M., Koval, L., Комісаренко, С. В., & Skok, M. V. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.05.018 · Cited by 26
Yıldız, H., Hakan, H., Ekin, S., Arisoy, A., Günbatar, H., Aşker, S., Çi̇̇li̇̇ngi̇̇r, B. M., Sunnetcioglu, A., ÇELİKEL, M., Esen, N., et al. (2021) · Infectious Diseases Now · doi:10.1016/j.idnow.2021.06.302 · Cited by 26
“The novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first identified in China and spread throughout the world within a few months, resulting in a pandemic [1].”
BackgroundRavichandran, B., Grimm, D. G., Krüger, M., Kopp, S., Infanger, M., & Wehland, M. (2021) · Physiological Reports · doi:10.14814/phy2.14800 · Cited by 28
Evolution, correlation, structural impact and dynamics of emerging SARS-CoV-2 variants
Spratt, A. N., Kannan, S. R., Woods, L. T., Weisman, G. A., Quinn, T. P., Lorson, C. L., Sönnerborg, A. B., Byrareddy, S. N., & Singh, K. D. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.06.037 · Cited by 25
Choi, H.-I., Kim, T., Lee, S., Kim, J. W., Noh, Y. J., Kim, G., Park, H. J., Chae, Y., Lee, K., Kim, S., et al. (2021) · Journal of Chromatography B · doi:10.1016/j.jchromb.2021.122862 · Cited by 26
SARS-CoV-2 S glycoprotein binding to multiple host receptors enables cell entry and infection
Trbojević‐Akmačić, I., Petrović, T., & Lauc, G. (2021) · Glycoconjugate Journal · doi:10.1007/s10719-021-10021-z · Cited by 26
ACE2 in the Gut: The Center of the 2019-nCoV Infected Pathology
Guo, Y., Wang, B., Gao, H., Gao, L., Hua, R., & Xu, J. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.708336 · Cited by 26
Xiong, J., Xiang, Y., Huang, Z., Liu, X., Wang, M., Ge, G., Chen, H., Xu, J., Zheng, M., & Chen, L. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.740702 · Cited by 26
“In humans, the primary receptor of the SARS-CoV-2 spike protein is angiotensin-converting enzyme 2 (ACE2) (Wang et al., 2020; Zhang H. et al., 2020).”
BackgroundAntiviral and antibacterial activity of hand sanitizer and surface disinfectant formulations
Filipe, H. A. L., Fiuza, S. M., Henriques, C. A., & Antunes, F. E. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.121139 · Cited by 30
Human semen quality as affected by SARS‐CoV‐2 infection: An up‐to‐date review
Banihani, S. A. (2021) · Andrologia · doi:10.1111/and.14295 · Cited by 25
Protein-Based Nanoparticle Vaccines for SARS-CoV-2
Sung, H.-D., Kim, N., Lee, Y., & Lee, E. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413445 · Cited by 28
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“Most of the 15 mutation sites, including N501Y, G496S, K417N, Q493R, and G446S, are located in the loop regions of the ACE2-binding surface (Wang et al., 2020) (Figure 3A).”
Molecular Insights into the Differential Dynamics of SARS-CoV-2 Variants of Concern (VOC)
Mandal, N., Padhi, A. K., & Rath, S. L. (2021) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2022.108194 · Cited by 28
“The initial coordinates of the RBD/ACE2 complex were taken from the crystal structure (PDB ID: 6LZG) [24].”
MethodCreutznacher, R., Maaß, T., Veselková, B., Ssebyatika, G. L., Krey, T., Empting, M., Tautz, N., Frank, M., Kölbel, K., Uetrecht, C., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c05603 · Cited by 26
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Development and application of ribonucleic acid therapy strategies against COVID-19
Lin, N., Liu, M., Gou, Y., Yang, Y., He, B., & Huang, J. H. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.72706 · Cited by 26
“S1 could directly contact with the host receptor ACE2 with its receptor-binding domain (RBD), while the fusion and entrance of the following membrane to the host cytoplasm of the viruses were mediated by S2 subunit [54-58].”
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The multiple roles of nsp6 in the molecular pathogenesis of SARS-CoV-2
Bills, C. J., Xie, X., & Shi, P. (2023) · Antiviral Research · doi:10.1016/j.antiviral.2023.105590 · Cited by 30
SARS-CoV-2 Binding to Terminal Sialic Acid of Gangliosides Embedded in Lipid Membranes
Negi, G., Sharma, A., Chaudhary, M., Gupta, D., Harshan, K. H., & Parveen, N. (2023) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.3c00106 · Cited by 26
A pan-coronavirus peptide inhibitor prevents SARS-CoV-2 infection in mice by intranasal delivery
Wu, L., Zheng, A., Tang, Y., Chai, Y., Chen, J., Cheng, L., Hu, Y., Qu, J. T., Lei, W., Liu, W. J., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2410-5 · Cited by 26
“S1 contains the RBD, which recognizes the cellular receptor angiotensin-converting enzyme 2 (ACE2) (Wang et al., 2020).”
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Kozłowski, P., Leszczyńska, A., & Ciepiela, O. (2024) · American Journal of Medicine Open · doi:10.1016/j.ajmo.2024.100068 · Cited by 27
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“The recombination evidence spans across SARS-CoV-2 S glycoprotein two subunits (S1 and S2), that share structural homology to its SARS-CoV-1 counterpart [29].”
BackgroundMinerals in biology and medicine
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Herbal Medicines to Fight Against COVID-19: New Battle with an Old Weapon
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SARS-CoV-2: An Overview of Virus Genetics, Transmission, and Immunopathogenesis
Farrag, M. A., Amer, H. M., Bhat, R., Hamed, M. E., Aziz, I. M., Mubarak, A., Dawoud, T. M. S., Almalki, S. G., Alghofaili, F., Alnemare, A. K., et al. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18126312 · Cited by 28
Up State of the SARS-COV-2 Spike Homotrimer Favors an Increased Virulence for New Variants
Giron, C. C., Laaksonen, A., & da Silva, F. L. B. (2021) · Frontiers in Medical Technology · doi:10.3389/fmedt.2021.694347 · Cited by 25
“Indeed, it was noted before that SARS-CoV-1 and 2 (wt) are antigenically different (120).”
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“lular receptor protein angiotensin-converting enzyme 2 (ACE2), and S2 accounts for membrane fusion of virus and host cell [25,26].”
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Self-citationExpression pattern and function of SARS-CoV-2 receptor ACE2
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Khan, A., Hussain, S., Ahmad, S., Suleman, M., Bukhari, I., Khan, T., Rashid, F., Azad, A. K., Waseem, M., Khan, W., et al. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.105163 · Cited by 25
“Previous research have found that evaluating the binding of SARS-CoV-2 and SARS-CoV RBDs with ACE2 indicated stronger hydrogen bonds and electrostatic interactions in SARS-CoV-2 [26,49].”
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Methylxanthines as Potential Inhibitor of SARS-CoV-2: an In Silico Approach
Rolta, R., Salaria, D., Sharma, B., Awofisayo, O., Fadare, O. A., Sharma, S., Patel, C., Kumar, V., Sourirajan, A., Baumler, D. J., et al. (2022) · Current Pharmacology Reports · doi:10.1007/s40495-021-00276-3 · Cited by 25
“The crystal structures of three SARS CoV-2 proteins were downloaded in pdb format from the protein databank, namely nucleocapsid protein N-terminal RNA binding domain (PDB ID: 6M3M) [22], main protease (6LU7) [23] and spike receptor-binding domain (PDB ID: 6LZG) [24].”
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“The SARS-CoV-2 infection begins when virus particles attach to host cells due to interactions between S1 and ACE2 (Lan et al., 2020; Walls et al., 2020; Wang et al., 2020; Wrapp et al., 2020).”
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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