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Receptor Recognition by the Novel Coronavirus from Wuhan: an Analysis Based on Decade-Long Structural Studies of SARS Coronavirus
Open accessAbstract
The recent emergence of Wuhan coronavirus (2019-nCoV) puts the world on alert. 2019-nCoV is reminiscent of the SARS-CoV outbreak in 2002 to 2003. Our decade-long structural studies on the receptor recognition by SARS-CoV have identified key interactions between SARS-CoV spike protein and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of SARS-CoV. One of the goals of SARS-CoV research was to build an atomic-level iterative framework of virus-receptor interactions to facilitate epidemic surveillance, predict species-specific receptor usage, and identify potential animal hosts and animal models of viruses. Based on the sequence of 2019-nCoV spike protein, we apply this predictive framework to provide novel insights into the receptor usage and likely host range of 2019-nCoV. This study provides a robust test of this reiterative framework, providing the basic, translational, and public health research communities with predictive insights that may help study and battle this novel 2019-nCoV.
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“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“RBD contains a core structure and a variable receptor-binding motif (RBM; 437–508 a.a.) which interacts and attaches with the host cell ACE-2 receptor (Fig. 2) [7].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [7]
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969 · cited 1×
“Our structural analyses confidently predict that 2019-nCoV uses ACE2 as its host receptor, consistent with two other new publications (30, 31).”
ResultFast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · cited 1×
“Protein sequence alignments were done using Clustal Omega (33).”
MethodAngiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923 · cited 2×
“2) but is ancestral to both human SARS-CoV (epidemic strain isolated in year 2002) and bat SARS-CoV strains that use ACE2 receptor to enter and infect primary host lung cells (11, 17).”
BackgroundOrigin and evolution of pathogenic coronaviruses
Cui, J., Li, F., & Shi, Z. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0118-9 · Cited by 5,729 · cited 2×
“It is believed that bats and palm civets were the natural and intermediate reservoirs for SARS-CoV, respectively, and that SARS-CoV transmitted from palm civets to humans in an animal market in Southern China (12–14).”
BackgroundSelf-citationLetko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Coronavirus as a possible cause of severe acute respiratory syndrome
Peiris, M. J. S., Lai, S., Poon, L. L. M., Guan, Y., Yam, L., Lim, W., Nicholls, J. M., Yee, W., Yan, W., Cheung, M., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)13077-2 · Cited by 2,916
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740 · cited 1×
“An envelope-anchored spike protein mediates coronavirus entry into host cells by first binding to a host receptor and then fusing viral and host membranes (16).”
BackgroundSelf-citationA Major Outbreak of Severe Acute Respiratory Syndrome in Hong Kong
Lee, N. L. S., Hui, D. S. C., Wu, A. K. L., Chan, P. K. S., Cameron, P. A., Joynt, G. M., Ahuja, A. T., Yung, M. Y., Leung, C. B., To, K. F., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030685 · Cited by 2,638
Guan, Y., Zheng, B., He, Y., Liu, X. L., Zhuang, Z. X., Cheung, C. L., Luo, S., Li, P. H., Zhang, L., Guan, Y., et al. (2003) · Science · doi:10.1126/science.1087139 · Cited by 2,404
Cited by
Sorted by citations
Items 401–500 of 1,004
Epigenetic mechanisms regulating COVID-19 infection
Chlamydas, S., Papavassiliou, A. G., & Piperi, C. (2020) · Epigenetics · doi:10.1080/15592294.2020.1796896 · Cited by 135
“Human ACE2 contains two hot spots for virus binding and mutations at the RBM occurring naturally near these hot spots, determine the host range of the virus [20] (Figure 1b,c).”
BackgroundRole of Genetic Variants and Gene Expression in the Susceptibility and Severity of COVID-19
Choudhary, S., Sreenivasulu, K., Mitra, P., Misra, S., & Sharma, P. (2020) · Annals of Laboratory Medicine · doi:10.3343/alm.2021.41.2.129 · Cited by 140
“the SARS-CoV binding and could also abolish the interaction [31].”
BackgroundTejerina, F., Catalán, P., Rodríguez‐Grande, C., Adán‐Jiménez, J., Rodríguez, C., Muñóz, P., Aldámiz‐Echevarría, T., Díez, C., Latorre, L. P., Fanciulli, C., et al. (2022) · BMC Infectious Diseases · doi:10.1186/s12879-022-07153-4 · Cited by 135
“SARS and SARS-CoV-2 bind to the angiotensin-converting enzyme 2 receptor (ACE2) to enter the cells [7, 8].”
BackgroundPandey, A., Nikam, A. N., Shreya, A. B., Mutalik, S. P., Gopalan, D., Kulkarni, S., Padya, B. S., Fernandes, G. J., Mutalik, S., & Prassl, R. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117883 · Cited by 132
“Receptor affinity analysis claims that the SARS-CoV strain binds less efficiently than the novel SARS-CoV-2 strain, and further mutation in the nucleotide sequence of RBD may increase its pathogenicity [17].”
Vishnubalaji, R., Shaath, H., & Alajez, N. M. (2020) · Genes · doi:10.3390/genes11070760 · Cited by 130
“In fact, nine out of the 14 residues in the RBD of SARS-CoV are conserved in human through bat [16].”
BackgroundIn-Silico Evidence for a Two Receptor Based Strategy of SARS-CoV-2
Milanetti, E., Miotto, M., Rienzo, L. D., Nagaraj, M., Monti, M., Golbek, T. W., Gosti, G., Roeters, S. J., Weidner, T., Otzen, D. E., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.690655 · Cited by 133
“2 Identification of Another Possible Binding Region of the SARS-CoV-2 Spike Although it is currently known that the spike protein of SARSCoV-2 binds to the ACE2 receptor of host cells (Hoffmann et al., 2020; Wan et al., 2020), the investigation of possible other infection mechanisms is important in the study of this d…”
BackgroundOshaghi, E. A., Mirzaei, F., Farahani, F., Khodadadi, I., & Tayebinia, H. (2020) · International Journal of Surgery · doi:10.1016/j.ijsu.2020.05.018 · Cited by 133
Zhang, G., Nie, S., Zhang, Z., & Zhang, Z. (2020) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiaa229 · Cited by 133
COVID-19 research: pandemic versus “paperdemic”, integrity, values and risks of the “speed science”
Dinis‐Oliveira, R. J. (2020) · Forensic Sciences Research · doi:10.1080/20961790.2020.1767754 · Cited by 137
“But where is the science behind the publications on this subject? Firstly, it was demonstrated that SARS-CoV-2 binds to its target cells through angiotensin-converting enzyme 2 (ACE2), which is expressed by epithelial cells of the lung, intestine, kidney, and blood vessels [104].”
BackgroundSinha, S. K., Prasad, S. K., Islam, M. A., Gurav, S. S., Patil, R. B., AlFaris, N. A., Aldayel, T. S., AlKehayez, N. M., Wabaidur, S. M., & Shakya, A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1779132 · Cited by 132
“A two-step sequential protease cleavage starts with activation of S proteins CoVs, which involves prime cleavage between two subunits (i.e. S1 and S2) and activates cleavage on S2’ site (Belouzard et al., 2009; Cotten et al., 2013; Ou et al., 2020; Wan et al., 2020).”
BackgroundExpression of ACE2 in Human Neurons Supports the Neuro-Invasive Potential of COVID-19 Virus
Xu, J., & Lazartigues, E. D. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00915-1 · Cited by 132
“Similar to SARS-CoV, which caused the SARS epidemic in 2002–2003, SARS-CoV-2 also binds to angiotensin-converting enzyme 2 (ACE2) in the lung to enter pulmonary cells, via its S1 spike protein (Wan et al. 2020), yet the S protein of SARS-CoV-2 exhibits higher affinity to ACE2 (Wrapp et al.”
ResultNaz, A., Shahid, F., Butt, T. T., Awan, F. M., Ali, A., & Malik, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01663 · Cited by 130
Mackey, K., King, V. J., Gurley, S. B., Kiefer, M., Liederbauer, E., Vela, K., Sonnen, P., & Kansagara, D. L. (2020) · Annals of Internal Medicine · doi:10.7326/m20-1515 · Cited by 130
“The concern about ACEI or ARB use in patients with COVID-19 stemmed largely from arguments of biologic plausibility, particularly the observation that ACEIs and ARBs have the potential to upregulate ACE2 receptors (which seem to be the cellular entry point for SARS-CoV-2) (5).”
BackgroundInfluentialD-dimer as an indicator of prognosis in SARS-CoV-2 infection: a systematic review
Vidali, S., Morosetti, D., Cossu, E., Luisi, M., Pancani, S., Semeraro, V., & Consales, G. (2020) · ERJ Open Research · doi:10.1183/23120541.00260-2020 · Cited by 133
A Comprehensive Review About SARS-CoV-2
Haque, S. M., Ashwaq, O., Sarief, A., & Azad John Mohamed, A. K. (2020) · Future Virology · doi:10.2217/fvl-2020-0124 · Cited by 121
South, A. M., Brady, T. M., & Flynn, J. T. (2020) · Hypertension · doi:10.1161/hypertensionaha.120.15291 · Cited by 138
Mohapatra, R. K., Pintilie, L., Kandi, V., Sarangi, A. K., Das, D., Sahu, R., & Perekhoda, L. O. (2020) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13761 · Cited by 132
Recent progress in translational engineered in vitro models of the central nervous system
Nikolakopoulou, P., Rauti, R., Voulgaris, D., Shlomy, I., Maoz, B. M., & Herland, A. (2020) · Brain · doi:10.1093/brain/awaa268 · Cited by 133
“Certainly, SARS-CoV-2 research is at an immature state and the involvement of the CNS in disease progression is largely ambiguous (Li et al. , 2020 a , b ; Turtle, 2020).”
Scheller, C., Krebs, F., Minkner, R., Astner, I., Gil‐Moles, M., & Wätzig, H. (2020) · Electrophoresis · doi:10.1002/elps.202000121 · Cited by 130
Jehi, L. E., Ji, X., Milinovich, A., ERZURUM, S. C., Merlino, A. A., Gordon, S., Young, J. B., & Kattan, M. W. (2020) · PLoS ONE · doi:10.1371/journal.pone.0237419 · Cited by 125
COVID-19 and Cancer Comorbidity: Therapeutic Opportunities and Challenges
Pathania, A. S., Prathipati, P., Abdul, B. A., Chava, S. P., Katta, S. S., Gupta, S. C., Gangula, P. R., Pandey, M. K., Durden, D. L., Byrareddy, S. N., et al. (2020) · Theranostics · doi:10.7150/thno.51471 · Cited by 131
“erythematosus, systemic lupus erythematosus in adults, and rheumatoid arthritis [109].”
BackgroundMercurio, I., Tragni, V., Busto, F., Grassi, A., & Pierri, C. L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03580-1 · Cited by 129
“The reported data represents an updated/integrated analysis of a similar ones reported in (53), in light of the recently deposited SARS-CoV-2 spike RBD in complex with the human ACE2 (6vw1.”
ResultTazerji, S. S., Duarte, P. M., Rahimi, P., Shahabinejad, F., Dhakal, S., Malik, Y. S., Shehata, A. A., Lama, J., Klein, J., Safdar, M., et al. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02534-2 · Cited by 126
“Because it has a similar genome to other animal coronaviruses, SARSCoV-2 may have undergone nucleotide mutation when transmitted to animals, expressing amino acids that increased its pathogenicity in animals, especially those related to spike protein [38, 39].”
BackgroundUnraveling the Possible Routes of SARS-COV-2 Invasion into the Central Nervous System
Lima, M., Siokas, V., Aloizou, A., Liampas, I., Mentis, A. A., Tsouris, Z., Papadimitriou, A., Mitsias, P. D., Tsatsakis, A. M., Bogdanos, D. P., et al. (2020) · Current Treatment Options in Neurology · doi:10.1007/s11940-020-00647-z · Cited by 129
Li, R., Qiao, S., & Zhang, G. (2020) · Journal of Infection · doi:10.1016/j.jinf.2020.02.013 · Cited by 125
A hypothesized role for dysregulated bradykinin signaling in COVID‐19 respiratory complications
Roche, J. A., & Roche, R. (2020) · The FASEB Journal · doi:10.1096/fj.202000967 · Cited by 127
Coronavirus disease 2019 and cardiovascular system: A narrative review
Kwenandar, F., Japar, K. V., Damay, V., Hariyanto, T. I., Tanaka, M. S., Lugito, N. P. H., & Kurniawan, A. (2020) · IJC Heart & Vasculature · doi:10.1016/j.ijcha.2020.100557 · Cited by 126
“Furthermore, two experimental studies proved that SARS-CoV-2 uses ACE2, which is also expressed in the heart, as their receptor for entry into the cell [17,18].”
Pathophysiology and treatment strategies for COVID-19
Kumar, M., & Khodor, S. A. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-020-02520-8 · Cited by 123
“SARS-CoV-2 binds to host cells through the ACE2 receptor, which is expressed by epithelial cells of the lungs, intestines, kidneys, brain, and blood vessels [29].”
BackgroundAntiviral strategies targeting host factors and mechanisms obliging +ssRNA viral pathogens
Mahajan, S., Choudhary, S., Kumar, P., & Tomar, S. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116356 · Cited by 127
Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants
Mittal, A., Khattri, A., & Verma, V. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010260 · Cited by 124
“Though N501 is one of the key residues that increases the RBD-ACE2 binding affinity [32,52], but the N501Y mutation has been shown to improve the binding affinity in vitro by hydrophobic interactions of the RBD Y501 with ACE2 Y41, and favorable cation–π stacking interactions with ACE2 K353 [21,53,54].”
BackgroundPharmacotherapy in COVID-19; A narrative review for emergency providers
Mehta, N., Mazer-Amirshahi, M. E., Alkindi, N., & Pourmand, A. (2020) · The American Journal of Emergency Medicine · doi:10.1016/j.ajem.2020.04.035 · Cited by 122
“Structural studies of SARS-CoV-1 and -2 have indicated that the viruses are able to bind to their target human cells by using ACE2 as their receptor [37].”
A global treatments for coronaviruses including COVID‐19
Yousefi, B., Valizadeh, S., Ghaffari, H., Vahedi, A., Karbalaei, M., & Eslami, M. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29785 · Cited by 120
Coronaviruses in wastewater processes: Source, fate and potential risks
Amoah, I. D., Kumari, S., & Bux, F. (2020) · Environment International · doi:10.1016/j.envint.2020.105962 · Cited by 123
Fodor, A., Tiperciuc, B., Login, C., Orasan, O. H., Lazăr, A.-L., Buchman, C., Hanghicel, P., Sitar-Tăut, A., Suharoschi, R., Vulturar, R., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8671713 · Cited by 127
Cholesterol-Rich Lipid Rafts as Platforms for SARS-CoV-2 Entry
Palacios-Rápalo, S. N., Jesús‐González, L. A. D., Cordero‐Rivera, C. D., Farfán-Morales, C. N., Osuna‐Ramos, J. F., Martínez-Mier, G., Quistián-Galván, J., Muñoz-Pérez, A., Bernal-Dolores, V., del Ángel, R. M., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.796855 · Cited by 125
“allowing fusion between cell and viral membranes (13, 51, 52).”
BackgroundFirst clinical study using HCV protease inhibitor danoprevir to treat COVID-19 patients
Chen, H., Zhang, Z., Wang, L., Huang, Z., Gong, F., Li, X., Chen, Y., & Wu, J. J. (2020) · Medicine · doi:10.1097/md.0000000000023357 · Cited by 122
“During SARS-COV-2’s life cycle, chymotrypsin-like protease (3CL pro) can cleave viral polyprotein to form the RNA replicase–transcriptase complex, which is essential for both viral transcription and replication.([7,8]) The proteases of HCV and human immunodeficiency virus (HIV) showed similar function as SARS-COV-2, s…”
Dengue Fever, COVID ‐19 ( SARS‐CoV ‐2), and Antibody‐Dependent Enhancement ( ADE ): A Perspective
Ulrich, H., Pillat, M. M., & Tárnok, A. (2020) · Cytometry Part A · doi:10.1002/cyto.a.24047 · Cited by 122
“This interpretation conflicts with experimental results from Ou et al.(41), who found that antisera from recovered SARS or COVID-19 patients had only limited cross neutralization effects of 293/hACE2 cells’ infection with SARS-CoV S or SARS-CoV-2 S pseudovirons.”
BackgroundInfluentialCOVID-19 and the Kidney: From Epidemiology to Clinical Practice
Gagliardi, I., Patella, G., Michael, A., Serra, R., Provenzano, M., & Andreucci, M. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082506 · Cited by 124
“found that the SARS-CoV-2 RBD has a single mutation that improves its binding affinity with ACE-2 [59].”
BackgroundMolecular Investigation of SARS–CoV-2 Proteins and Their Interactions with Antiviral Drugs
Calligari, P. A., Bobone, S., Ricci, G., & Bocedi, A. (2020) · Viruses · doi:10.3390/v12040445 · Cited by 123
Emerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
Thye, A. Y.-K., Law, J. W., Pusparajah, P., Letchumanan, V., Chan, K., & Lee, L. (2021) · Biomedicines · doi:10.3390/biomedicines9101303 · Cited by 121
“Furthermore, various naturally selected mutations in the RBM have been associated with human-to-human transmission, pathogenesis, infectivity, and immune escape [102].”
BackgroundEvolutionary and Structural Insights about Potential SARS-CoV-2 Evasion of Nirmatrelvir
Yang, K. S., Leeuwon, S. Z., Xu, S., & Liu, W. R. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00404 · Cited by 120
Repurposing Drugs, Ongoing Vaccine, and New Therapeutic Development Initiatives Against COVID-19
Saha, R. P., Sharma, A. R., Singh, M. K., Samanta, S., Bhakta, S., Mandal, S., Bhattacharya, M., Lee, S. S., & Chakraborty, C. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01258 · Cited by 118
The genetic structure of SARS‐CoV‐2 does not rule out a laboratory origin
Segreto, R., & Deigin, Y. (2020) · BioEssays · doi:10.1002/bies.202000240 · Cited by 126
“,[49] SARS-CoV-2 has the potential to recognize hACE2 more efficiently than the SARS-CoV, which emerged in 2002.”
BackgroundScavenger receptors in host defense: from functional aspects to mode of action
Taban, Q., Mumtaz, P. T., Masoodi, K. Z., Haq, E., & Ahmad, S. M. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-021-00812-0 · Cited by 136
Singh, R., Bhardwaj, V. K., Sharma, J., Kumar, D., & Purohit, R. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104631 · Cited by 117
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain
Ye, G., Liu, B., & Li, F. (2022) · Nature Communications · doi:10.1038/s41467-022-28882-9 · Cited by 121
Self-citationRathnasinghe, R., Jangra, S., Čupić, A., Martínez‐Romero, C., Mulder, L. C. F., Kehrer, T., Yildiz, S., Choi, A., Mena, I., Vrieze, J. D., et al. (2021) · medRxiv · doi:10.1101/2021.01.19.21249592 · Cited by 110
Fruitful Neutralizing Antibody Pipeline Brings Hope To Defeat SARS-Cov-2
Renn, A., Fu, Y., Hu, X., Hall, M. D., & Simeonov, A. M. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.07.004 · Cited by 117
“Further, two other analyses of SARS-CoV-2 have suggested a trend towards enhanced structural stability as well as higher af fi nity for ACE2, and this may indicate acquired increased infectivity during the pandemic [82 – 84].”
Teng, S., Sobitan, A., Rhoades, R. E., Liu, D., & Tang, Q. (2020) · Briefings in Bioinformatics · doi:10.1093/bib/bbaa233 · Cited by 117
“It regulates the S protein folding, increases its stability and has wide-ranging roles in viral pathobiology, including mediating, and shaping viral tropism (9).”
Optimization and evaluation of propolis liposomes as a promising therapeutic approach for COVID-19
Refaat, H., Mady, F. M., Sarhan, H. A., Rateb, H. S., & Alaaeldin, E. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.120028 · Cited by 122
“ACE II has been proven to be strongly recognized by SARS-CoV-2 than SARS CoV (Wan et al., 2020), hence increasing the opportunity to be transmitted from person to person.”
Animal Models for COVID-19: Hamsters, Mouse, Ferret, Mink, Tree Shrew, and Non-human Primates
Shou, S., Liu, M., Yang, Y., Kang, N., Song, Y., Tan, D., Liu, N., Wang, F., Liu, J., & Xie, Y. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.626553 · Cited by 120
Zabidi, N. Z., Liew, H. L., Farouk, I. A., Puniyamurti, A., Yip, A. J. W., Wijesinghe, V. N., Low, Z. Y., Tang, J. W.-T., Chow, V. T. K., & Lal, S. K. (2023) · Viruses · doi:10.3390/v15040944 · Cited by 129
Karimi, S., Arabi, A., Shahraki, T., & Safi, S. (2020) · Eye · doi:10.1038/s41433-020-0965-2 · Cited by 116
Shiers, S. I., Ray, P. R., Wangzhou, A., Sankaranarayanan, I., Tatsui, C. E., Rhines, L. D., Li, Y., Uhelski, M. L., Dougherty, P. M., & Price, T. J. (2020) · Pain · doi:10.1097/j.pain.0000000000002051 · Cited by 116
Plasma ACE2 predicts outcome of COVID-19 in hospitalized patients
Kragstrup, T. W., Singh, H. S., Grundberg, I., Nielsen, A. L., Rivellese, F., Mehta, A., Goldberg, M. B., Filbin, M. R., Qvist, P., & Bibby, B. M. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252799 · Cited by 117
Saliva—Friend and Foe in the COVID-19 Outbreak
Han, P., & Ivanovski, S. (2020) · Diagnostics · doi:10.3390/diagnostics10050290 · Cited by 115
“Of note, the spike protein is the glyc pr tein that facilitates SARS-CoV-2 attachme t, fusion, entry, and transmission into host cells by binding with human angiotensin converting enzyme 2 (hACE2) receptors [19], which are expressed by epithelial cells of the lung, intestine, kidney, blood vessels, and oral mucosa [20…”
BackgroundRole of Monocytes/Macrophages in Covid-19 Pathogenesis: Implications for Therapy
Rial, J. G., Calle, I. R., Salas, A., & Martinón‐Torres, F. (2020) · Infection and Drug Resistance · doi:10.2147/idr.s258639 · Cited by 122
Small molecules in the treatment of COVID-19
Lei, S., Chen, X., Wu, J., Duan, X., & Men, K. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01249-8 · Cited by 119
“6).137,138 In human ACE2, Lys-31 and Lys-353 are sensitive to the RBD.139 Its glycosylation sites Asn-90 and Asn-322 also demonstrated the ability to interfere with S protein binding in a recent study.140 Glycosylation of asparagine residues within the RBD is an important mediator of ACE2 binding.141 The effects of mo…”
BackgroundInfluentialZhao, X., Wang, K., Zuo, P., Liu, Y., Zhang, M., Xie, S., Zhang, H., Chen, X., & Liu, C. (2020) · The EPMA Journal · doi:10.1007/s13167-020-00208-z · Cited by 112
“SARS-CoV-2 can bind to its target cells through angiotensin-converting enzyme 2 (ACE2) [22], which would Data were mean ± SD, n (%). p values comparing groups were from Student’s t test for continuous data and chi-squared tests for categorical variables facilitate infection with COVID-19, while hypertension and diabet…”
BackgroundInfluentialEnhanced Binding of SARS-CoV-2 Spike Protein to Receptor by Distal Polybasic Cleavage Sites
Qiao, B., & de la Cruz, M. O. (2020) · ACS Nano · doi:10.1021/acsnano.0c04798 · Cited by 110
Alluwaimi, A. M., Alshubaith, I. H., Al-Ali, A. M., & Abohelaika, S. (2020) · Frontiers in Veterinary Science · doi:10.3389/fvets.2020.582287 · Cited by 113
Cho, S. I., Yoon, S., & Lee, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-85813-2 · Cited by 122
Jung, S., Choi, J. C., You, S., & Kim, W. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa624 · Cited by 116
Impact of Diabetes in Patients Diagnosed With COVID-19
Abu‐Farha, M., Al‐Mulla, F., Thanaraj, T. A., Kavalakatt, S., Ali, H., Ghani, M. A., & Abubaker, J. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.576818 · Cited by 122
“Studies have reported that the expression of ACE2 is elevated in people with diabetes treated with these medications (79, 80).”
BackgroundCOVID-19 pandemic crisis and food safety: Implications and inactivation strategies
Han, S., Roy, P. K., Hossain, M. I., Byun, K.-H., Choi, C., & Ha, S. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.01.004 · Cited by 113
Hypertension and Diabetes Delay the Viral Clearance in COVID-19 PatientsPreprint
Chen, X., Hu, W., Ling, J., Mo, P., Zhang, Y., Jiang, Q., Ma, Z., Cao, Q., Deng, L., Song, S., et al. (2020) · medRxiv · doi:10.1101/2020.03.22.20040774 · Cited by 120
Progress and Concept for COVID‐19 Vaccine Development
Wu, S. (2020) · Biotechnology Journal · doi:10.1002/biot.202000147 · Cited by 114
SARS-CoV-2 Vaccine Development: Current Status
Poland, G. A., Ovsyannikova, I. G., Crooke, S. N., & Kennedy, R. B. (2020) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2020.07.021 · Cited by 119
“24,25 As per a recent case report, the increased frequency of antibody-secreting cells, follicular helper T cells, activated CD38þHLA-DRþCD8þ andCD4þT lymphocytes, togetherwith SARS-CoV-2especific IgG and IgM antibodies, detected in the blood of a Mayo Clin Proc. n October 2020;9 patient with nonsevere COVID-19 prior…”
BackgroundInfluentialComparing the Binding Interactions in the Receptor Binding Domains of SARS-CoV-2 and SARS-CoV
Amin, M., Sorour, M. K., & Kasry, A. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c01064 · Cited by 114
In silico design of antiviral peptides targeting the spike protein of SARS-CoV-2
Ling, R., Dai, Y., Huang, B., Huang, W., Yu, J., Lu, X., & Jiang, Y.-Z. (2020) · Peptides · doi:10.1016/j.peptides.2020.170328 · Cited by 112
Thachil, J. V., & Srivastava, A. (2020) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0040-1712155 · Cited by 111
Kaur, N., Singh, R., Dar, Z., Bijarnia, R. K., Dhingra, N., & Kaur, T. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104490 · Cited by 115
“Additionally, the genome of Rhinolophus affinis bat (Zhou et al., 2020b) was found to share 96% similarity to the novel coronavirus with non-homologous regions belonging to the RBD region of S protein suggesting incompatibility of this strain with human ACE2 receptor (Wan et al., 2020).”
Yu, Z., Kan, R., Ji, H., Wu, S., Zhao, W., Shuian, D., Liu, J., & Li, J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.128366 · Cited by 111
Hypoxic and Pharmacological Activation of HIF Inhibits SARS-CoV-2 Infection of Lung Epithelial Cells
Wing, P. A. C., Keeley, T. P., Zhuang, X., Lee, Y. S., Prange‐Barczynska, M., Tsukuda, S., Morgan, S. B., Harding, A. C., Argles, I. L. A., Kurlekar, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109020 · Cited by 108
“…tract and infection is mediated by spike (S) protein binding to the human angiotensin-converting enzyme 2 (ACE2), where the transmembrane protease serine 2 This is an open access article und (TMPRSS2) triggers fusion of the viral and cell membranes (Hoffmann et al., 2020; Wan et al., 2020).”
Polyunsaturated ω-3 fatty acids inhibit ACE2-controlled SARS-CoV-2 binding and cellular entry
Goc, A., Niedzwiecki, A., & Rath, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-84850-1 · Cited by 113
Shorter telomere lengths in patients with severe COVID-19 disease
Sánchez-Vazquez, R., Guío-Carrión, A., Zapatero, A., Martínez, P., & Blasco, M. A. (2021) · Aging · doi:10.18632/aging.202463 · Cited by 110
Risk of human‐to‐wildlife transmission of SARS‐CoV‐2
Gryseels, S., Bruyn, L. D., Gyselings, R., Calvignac‐Spencer, S., Leendertz, F. H., & Leirs, H. (2020) · Mammal Review · doi:10.1111/mam.12225 · Cited by 114
“These variations can affect the efficiency with which RBD binds to ACE2, and therefore ACE2 is a major determinant in a species’ susceptibility to SARS-CoV-2 [23].”
BackgroundCoronavirus Disease 2019 (COVID-19) and Nutritional Status: The Missing Link?
Silvério, R., Gonçalves, D. C., Andrade, M. F., & Seelaender, M. C. L. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa125 · Cited by 120
Tinti, F., Lai, S., Noce, A., Rotondi, S., Marrone, G., Mazzaferro, S., Daniele, N. D., & Mitterhofer, A. P. (2021) · Life · doi:10.3390/life11050419 · Cited by 117
“Strong evidence supports ACE2 as receptors for SARS-CoV-2, displayed on the principal target cells in the respiratory tract and lungs but also in the heart and kidney, in particular on glomerular and tubular cells [66].”
BackgroundGhosh, A. K., Raghavaiah, J., Shahabi, D., Yadav, M., Anson, B. J., Lendy, E. K., Hattori, S.-I., Higashi‐Kuwata, N., Mitsuya, H., & Mesecar, A. D. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01214 · Cited by 109
Garreta, E., Prado, P., Stanifer, M. L., Monteil, V., Marco, A., Ullate‐Agote, A., Moya‐Rull, D., Vilas‐Zornoza, A., Tarantino, C., Romero, J. P., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.04.009 · Cited by 112
LY6E Restricts Entry of Human Coronaviruses, Including Currently Pandemic SARS-CoV-2
Zhao, X., Zheng, S., Chen, D., Zheng, M., Li, X., Li, G., Lin, H., Chang, J., Zeng, H., & Guo, J. (2020) · Journal of Virology · doi:10.1128/jvi.00562-20 · Cited by 107
Advances in research on ACE2 as a receptor for 2019-nCoV
Wu, J., Deng, W., Li, S., & Yang, X. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03611-x · Cited by 114
The aging transcriptome and cellular landscape of the human lung in relation to SARS-CoV-2
Chow, R. D.-W., Majety, M., & Chen, S. (2021) · Nature Communications · doi:10.1038/s41467-020-20323-9 · Cited by 106
Factors Associated with Mortality in COVID-19 Patients: A Systematic Review and Meta-Analysis
Sepandi, M., Taghdir, M., Alimohamadi, Y., Afrashteh, S., & Hosamirudsari, H. (2020) · Iranian Journal of Public Health · doi:10.18502/ijph.v49i7.3574 · Cited by 107
“ACE2 is the host receptor of the COVID-19 virus (36, 37).”
BackgroundProbiotics: A potential immunomodulator in COVID-19 infection management
Singh, K., & Rao, A. (2021) · Nutrition Research · doi:10.1016/j.nutres.2020.12.014 · Cited by 109
Cennamo, N., D’Agostino, G., Perri, C., Arcadio, F., Chiaretti, G., Parisio, E. M., Camarlinghi, G., Vettori, C., Marzo, F. D., Cennamo, R., et al. (2021) · Sensors · doi:10.3390/s21051681 · Cited by 110
Isolation and characterization of cross-neutralizing coronavirus antibodies from COVID-19+ subjects
Jennewein, M. F., MacCamy, A. J., Akins, N. R., Feng, J., Homad, L. J., Hurlburt, N. K., Seydoux, E., Wan, Y.-H., Stuart, A. B., Edara, V. V., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109353 · Cited by 108
“In contrast, CV1-30 binds directly to the receptor binding motif which only has 50% sequence homology among SARS-CoV-1 and SARS-CoV-2 (Finkelstein et al., 2021; Hurlburt et al., 2020; Wan et al., 2020b).”
InfluentialSelf-citationIdentification of 2019-nCoV related coronaviruses in Malayan pangolins in southern ChinaPreprint
Lam, T. T., Shum, M. H.-H., Zhu, H., Tong, Y., Ni, X.-B., Liao, Y., Wei, W., Cheung, W. Y.-M., Li, W., Li, L., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.13.945485 · Cited by 116
Bottari, B., Castellone, V., & Neviani, E. (2020) · International Journal of Food Sciences and Nutrition · doi:10.1080/09637486.2020.1807475 · Cited by 112
“The expression of ACE2, which is expressed by epithelial cells of the lung, intestine, kidney, and blood vessels, is substantially increased in patients treated with ACE inhibitors (Wan et al. 2020).”
BackgroundChen, E. C., Gilchuk, P., Zost, S. J., Suryadevara, N., Winkler, E. S., Cabel, C. R., Binshtein, E., Chen, R. E., Sutton, R. E., Rodriguez, J. L., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109604 · Cited by 102
“SARS-CoV-2 and SARS-CoV-1 share approximately 80% amino acid sequence identity, and both use human angiotensin-converting enzyme 2 (ACE2) as an entry receptor through binding mediated by the RBD (Hoffmann et al., 2020; Li et al., 2003; Wan et al., 2020).”
The SARS-CoV-2 Coronavirus and the COVID-19 Outbreak
Lauxmann, M. A., Santucci, N. E., & Autrán-Gómez, A. M. (2020) · International braz j urol · doi:10.1590/s1677-5538.ibju.2020.s101 · Cited by 110
“Interestingly, five of these six amino acids differ between SARS-CoV-2 and SARS-CoV (26).”
BackgroundProbiotics at War Against Viruses: What Is Missing From the Picture?
Tiwari, S. K., Dicks, L. M. T., Popov, I. V., Karaseva, A. B., Ermakov, A. M., Suvorov, A. N., Tagg, J. R., Weeks, R. M., & Chikindas, M. L. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01877 · Cited by 109
“The origin of SARS-CoV-2 is highly debated (Guo et al., 2020; Paraskevis et al., 2020; Wan et al., 2020).”
BackgroundSmoking and COVID-19: Adding Fuel to the Flame
Kashyap, V. K., Dhasmana, A., Massey, A. E., Kotnala, S., Zafar, N., Jaggi, M., Yallapu, M. M., & Chauhan, S. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186581 · Cited by 108
“Based on sequencing and evolutionary data, bats are the currently proposed source reservoir for coronaviruses [2,3].”
BackgroundAnimal models for COVID-19: advances, gaps and perspectives
Fan, C., Wu, Y., Xiong, R., Yang, Y., Ling, C., Liu, S., Liu, S., & Wang, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01087-8 · Cited by 110
“Because the mouse ACE2 receptor does not support viral binding, wild-type mice are not permissive to SARS-CoV-2 infection.(170,245,246) To sensitize the wild-type mice, adeno associated vector or adenovirus 5 expressing hACE2 (AAV-hACE2, Ad5hACE2) were used to transduce mice intratracheally, causing hACE2 expression i…”
MethodDariya, B., & Nagaraju, G. P. (2020) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2020.05.001 · Cited by 105
“[69] also determined that SARS-CoV with residue 479 (lysine) and SARS-CoV-2 with glutamine 394 residue recognize and bind to lysine 31 of the ACE2 receptor in humans [70].”
Wang, R., Hozumi, Y., Yin, C., & Wei, G. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00501 · Cited by 104
Chilimuri, S. S., Sun, H., Alemam, A., Mantri, N., Shehi, E., Tejada, J., Yugay, A., & Nayudu, S. K. (2020) · Western Journal of Emergency Medicine · doi:10.5811/westjem.2020.6.47919 · Cited by 104
Khalifa, S. A. M., Yosri, N., El-Mallah, M. F., Ghonaim, R., Guo, Z., Musharraf, S. G., Du, M., Khatib, A., Xiao, J., Saeed, A., et al. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153311 · Cited by 106
Singh, H., Choudhari, R. H., Nema, V., & Khan, A. A. (2020) · Microbial Pathogenesis · doi:10.1016/j.micpath.2020.104621 · Cited by 106
Metadata
- Authors
- Wan, Y., Shang, J., Graham, R., Baric, R. S., & Li, F.
- Affiliations
- University of Minnesota (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Li, Fang
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2020-03-17
- Volume
- 94
- Issue
- 7
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC7081895
- OpenAlex
- W3004348779
- Cited by
- 4,341
- References
- 38
- Citations by year
- 2026: 27 · 2025: 75 · 2024: 170 · 2023: 299 · 2022: 619 · 2021: 1273 · 2020: 1865
- FWCI
- 133.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (R01AI089728, R01AI110700)
- 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 › Viral Infections and Outbreaks Research
- Keywords
- SARS-CoV-2, SARS-CoV, spike protein, angiotensin-converting enzyme 2, receptor recognition, host range prediction, interspecies transmission, human-to-human transmission, animal models, disease surveillance
- MeSH terms
- Protein Domains, Betacoronavirus, Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, Amino Acid Sequence, Animals, China, Chiroptera, Humans, Peptidyl-Dipeptidase A, Models, Molecular, Phylogeny, Pneumonia, Viral, Receptors, Virus, Sequence Alignment, Coronavirus Infections, Severe acute respiratory syndrome-related coronavirus, Host Specificity, Spike Glycoprotein, Coronavirus
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