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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 201–300 of 1,004
COVID-19: Virology, biology and novel laboratory diagnosis
Mohamadian, M., Chiti, H., Shoghli, A., Biglari, S., Parsamanesh, N., & Esmaeilzadeh, A. (2021) · The Journal of Gene Medicine · doi:10.1002/jgm.3303 · Cited by 371
Coronaviruses: a paradigm of new emerging zoonotic diseases
Salata, C., Calistri, A., Parolin, C., & Palù, G. (2019) · Pathogens and Disease · doi:10.1093/femspd/ftaa006 · Cited by 257
“A combination of modelling approaches and experimental evidence indicate that spikes of the 2019-nCoV recognize the ACE2 receptor, allowing entry into target cells (Letko and Munster 2020; Wan et al. 2020; Zhou et al. 2020).”
BackgroundLiu, Y., Hu, G., Wang, Y., Ren, W., Zhao, X., Ji, F., Zhu, Y., Feng, F., Gong, M., Ju, X., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025373118 · Cited by 247
“1 (bat), AB208708 (ferret), NM_001039456 (cat) (23).”
BackgroundMethodInfluentialDhama, K., Patel, S. K., Sharun, K., Pathak, M., Tiwari, R., Yatoo, M. I., Malik, Y. S., Sah, R., Rabaan, A. A., Panwar, P. K., et al. (2020) · Travel Medicine and Infectious Disease · doi:10.1016/j.tmaid.2020.101830 · Cited by 256
“The receptor-binding domain of the spike protein of SARS-CoV interacts with the host receptor ACE2 facilitating its potential of crossspecies, as well as human-to-human transmission [47].”
InfluentialGenomic determinants of pathogenicity in SARS-CoV-2 and other human coronaviruses
Gussow, A. B., Auslander, N., Faure, G., Wolf, Y. I., Zhang, F., & Koonin, E. V. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008176117 · Cited by 245
“The SARS-CoV-2 spike protein binds ACE2, the host cell receptor of SARS-CoV-2 (15), with a 10- to 20-fold greater affinity compared to SARS-CoV, and contains a polybasic furin cleavage site resulting from a unique insert to SARS-CoV-2 that could enhance infectivity (4).”
BackgroundInfluentialLi, Y., Renner, D. M., Comar, C. E., Whelan, J. N., Reyes, H. M., Cardenas‐Diaz, F. L., Truitt, R., Tan, L. H., Dong, B., Alysandratos, K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022643118 · Cited by 244
Singh, A. K., Gupta, R., & Misra, A. (2020) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2020.03.016 · Cited by 251
“Polymorphisms of ACE-2 gene have been identified; however, there is no evidence that they affect susceptibility to or severity of SARS CoV2 infection [29].”
InfluentialMultiple spillovers from humans and onward transmission of SARS-CoV-2 in white-tailed deer
Kuchipudi, S. V., Nair, M. S., Ruden, R. M., Yon, M., Nissly, R. H., Vandegrift, K. J., Nelli, R. K., Li, L., Jayarao, B. M., Maranas, C. D., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121644119 · Cited by 240
“SARS-CoV-2 uses the host angiotensin-converting enzyme 2 (ACE-2) receptor to enter cells (4).”
BackgroundMicrobiota Modulation of the Gut-Lung Axis in COVID-19
de Oliveira, G. L. V., Oliveira, C. N. S., Pinzan, C. F., de Salis, L. V. V., & Cardoso, C. R. D. B. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.635471 · Cited by 242
“The crucial step of the virus entry into the host organism is through the angiotensin converting enzyme 2 (ACE2) cell receptor (39, 40) and the successful infection also requires the transmembrane protease serine 2 (TMPRSS2), in a cleavage step of the viral Sprotein on the host cell membrane, thus allowing efficient v…”
BackgroundHamid, S., Mir, M. Y., & Rohela, G. K. (2020) · New Microbes and New Infections · doi:10.1016/j.nmni.2020.100679 · Cited by 249
Ortega, J. T., Serrano, M. L., Pujol, F. H., & Rangel, H. R. (2020) · EXCLI journal · doi:10.17179/excli2020-1167 · Cited by 244
“Strong scientific evidence showed that SARS and SARS-CoV-2 spike proteins interact with angiotensin-converting enzyme 2 (ACE2) (Chen et al 2020; Wan et al., 2020).”
BackgroundIs the kidney a target of SARS-CoV-2?
Martínez-Rojas, M. A., Vega‐Vega, O., & Bobadilla, N. A. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00160.2020 · Cited by 241
Zaki, N., Alashwal, H., & Ibrahim, S. (2020) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2020.07.005 · Cited by 248
Román, G. C., Gracia, F., Torres, A., Palacios, A., Gracia, K., & Harris, D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.653786 · Cited by 244
“IFN release can result in inflammation and immune system suppression (70).”
BackgroundMuus, C., Luecken, M. D., Eraslan, G., Waghray, A., Heimberg, G., Sikkema, L., Kobayashi, Y., Vaishnav, E. D., Subramanian, A., Smilie, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.19.049254 · Cited by 250
Dexamethasone for the Treatment of Coronavirus Disease (COVID-19): a Review
Ahmed, M. H., & Hassan, A. (2020) · SN Comprehensive Clinical Medicine · doi:10.1007/s42399-020-00610-8 · Cited by 239
“As proliferation of the virus occurs, the immune system is simultaneously attempting to expel it from the lungs, and, in some cases, causing immune-mediated damage of the pulmonary structures, in the process [22].”
BackgroundShen, Z., Ratia, K. M., Cooper, L. M., Kong, D., Lee, H., Kwon, Y., Li, Y., Alqarni, S., Huang, F., Dubrovskyi, O., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01307 · Cited by 237
Gastrointestinal and liver manifestations in patients with COVID-19
Lee, I., Huo, T., & Huang, Y. (2020) · Journal of the Chinese Medical Association · doi:10.1097/jcma.0000000000000319 · Cited by 231
“24 By analyzing endoscopic biopsy samples, Xiao et al 21 showed that ACE2 was rarely expressed in esophageal epithelium, but abundantly distributed in cilia of glandular epithelia, while staining of viral nucleocapsid protein was visualized in the cytoplasm of gastric, duodenal, and rectum…”
Resolution of coronavirus disease 2019 (COVID-19)
Habas, K., Nganwuchu, C. C., Shahzad, F., Gopalan, R. C., Haque, M., Rahman, S., Majumder, M. A. A., & Nasim, T. (2020) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2020.1797487 · Cited by 240
Nugraha, R. V., Ridwansyah, H., Ghozali, M., Khairani, A. F., & Atik, N. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/2560645 · Cited by 247
“respiratory tract, known as the angiotensin-converting enzyme-2 (ACE2) receptor [6].”
BackgroundInfluentialChoudhary, S., Malik, Y. S., & Tomar, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01664 · Cited by 231
“SARSCOV-2, a member of the Coronaviridae family, is a type of positive-sense, single-stranded enveloped RNA viruses responsible for causing infections in avian, mammalian and marine species across the world (1).”
BackgroundInfluentialDynamics of the ACE2–SARS-CoV-2/SARS-CoV spike protein interface reveal unique mechanisms
Ali, A., & Vijayan, R. (2020) · Scientific Reports · doi:10.1038/s41598-020-71188-3 · Cited by 238
Wuhan to World: The COVID-19 Pandemic
Kumar, A., Singh, R. G., Kaur, J., Pandey, S., Sharma, V., Thakur, L., Sati, S., Mani, S., Asthana, S., Sharma, T. K., et al. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.596201 · Cited by 247
Defining the Syrian hamster as a highly susceptible preclinical model for SARS-CoV-2 infection
Rosenke, K., Meade-White, K. D., Letko, M. C., Clancy, C. S., Hansen, F., Liu, Y., Okumura, A., Tang-Huau, T.-L., Li, R., Saturday, G. A., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1858177 · Cited by 216
“ing enzyme 2 (ACE-2) receptor has only low affinity for the SARS-CoV-2 spike protein leading to poor binding and entry [20,21].”
Zhu, Y., Yu, D., Yan, H., Chong, H., & He, Y. (2020) · Journal of Virology · doi:10.1128/jvi.00635-20 · Cited by 227
The role of extracellular vesicles in COVID-19 virus infection
Hassanpour, M., Rezaie, J., Nouri, M., & Panahi, Y. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104422 · Cited by 235
“…Lo Cigno et al., 2015 Glycoprotein B Antiviral Walker et al., 2009 Coronavirus CD9 Proviral Earnest et al., 2017; Jabbari et al., 2019; ACE2 Proviral Wan et al., 2020; Owczarek et al., 2018; Spike S protein Proviral Kuate et al., 2007 SGTM Proviral Kuate et al., 2007 a Kaposi's sarcoma-associated…”
BackgroundInfluentialHow can nanotechnology help to combat COVID-19? Opportunities and urgent need
Campos, E. V. R., Pereira, A. D. E. S., de Oliveira, J. L., Carvalho, L. B., Guilger‐Casagrande, M., de Lima, R., & Fraceto, L. F. (2020) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00685-4 · Cited by 234
“studies have shown that novel SARS-CoV-2 and SARSCoV infect host cells using the same angiotensin-converting enzyme 2 (ACE2) receptor [3, 11, 12].”
Age-Dependent Progression of SARS-CoV-2 Infection in Syrian Hamsters
Osterrieder, N., Bertzbach, L. D., Dietert, K., Abdelgawad, A., Vladimirova, D., Kunec, D., Hoffmann, D., Beer, M., Gruber, A. D., & Trimpert, J. (2020) · Viruses · doi:10.3390/v12070779 · Cited by 227
Robson, B. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.103670 · Cited by 228
Leroy, E. M., Gouilh, M. A., & Brugère‐Picoux, J. (2020) · One Health · doi:10.1016/j.onehlt.2020.100133 · Cited by 222
“While the Spike protein of SARS-CoV2 does bind well to the ACE2 of humans, ferrets, cats, and other species that have high receptor homology [20].”
BackgroundInfluentialNatural history of COVID-19 and current knowledge on treatment therapeutic options
dos Santos, W. G. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110493 · Cited by 235
Weston, S. M., Coleman, C. M., Haupt, R. E., Logue, J., Matthews, K. L., Li, Y., Reyes, H. M., Weiss, S. R., & Frieman, M. B. (2020) · Journal of Virology · doi:10.1128/jvi.01218-20 · Cited by 222
Intranasal fusion inhibitory lipopeptide prevents direct-contact SARS-CoV-2 transmission in ferrets
de Vries, R. D., Schmitz, K. S., Bovier, F. T., Predella, C., Khao, J., Noack, D., Haagmans, B. L., Herfst, S., Stearns, K. N., Drew-Bear, J., et al. (2021) · Science · doi:10.1126/science.abf4896 · Cited by 219
COVID-19 and the gastrointestinal tract: more than meets the eye
Ng, S. C., & Tilg, H. (2020) · Gut · doi:10.1136/gutjnl-2020-321195 · Cited by 219
“Akin to its relative SARS-CoV, SARS-CoV-2 uses Angiotensin converting enzyme)-2 (ACE2) as a viral receptor to enter host cells, [15] [16] [17] and ACE2 is an important regulator of intestinal inflammation.”
BackgroundMutations and Evolution of the SARS-CoV-2 Spike Protein
Magazine, N., Zhang, T., Wu, Y., McGee, M. C., Veggiani, G., & Huang, W. (2022) · Viruses · doi:10.3390/v14030640 · Cited by 225
“The RBD (~21 kDa) is responsible for the recognition of the angiotensin-converting enzyme 2 (ACE2) which acts as the receptor for SARS-CoV-2 viral entry [7].”
BackgroundQiu, Y., Zhao, Y., Wang, Q., Li, J., Zhou, Z., Liao, C.-H., & Ge, X. (2020) · Microbes and Infection · doi:10.1016/j.micinf.2020.03.003 · Cited by 217
“Among these sites, K31D, Y41A, Y83F, K353 H/A/D, D355A and R357A abolish or strongly inhibit SARS-CoV binding, while the substitutions on K68 and M383 slightly inhibit SARS-CoV binding [14,15].”
Acute myelitis after SARS-CoV-2 infection: a case reportPreprint
Zhao, K. F., Huang, J., Dai, D., Feng, Y., Liu, L., & Nie, S. (2020) · medRxiv · doi:10.1101/2020.03.16.20035105 · Cited by 217
D‐Dimer and Prothrombin Time Are the Significant Indicators of Severe COVID‐19 and Poor Prognosis
Long, H., Nie, L., Xiang, X., Li, H., Zhang, X., Fu, X., Ren, H., Liu, W., Wang, Q., & Wu, Q. (2020) · BioMed Research International · doi:10.1155/2020/6159720 · Cited by 219
“Upon SARS-CoV-2 entering the body through the angiotensin-converting enzyme 2 (ACE2) receptor adsorbed on the surface of mucosal epithelial cells [7, 8], its pathogenassociated molecular pattern (PAMP) can be quickly recognized by the immune system, and immune response is activated to clear the virus.”
BackgroundEvidence for SARS-CoV-2 Infection of Animal Hosts
Abdel-Moneim, A. S., & Abdelwhab, E. M. (2020) · Pathogens · doi:10.3390/pathogens9070529 · Cited by 209
Non-viral COVID-19 vaccine delivery systems
Park, K. S., Sun, X., Aikins, M. E., & Moon, J. J. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.12.008 · Cited by 216
“shares high sequence similarity with SARS-CoV and takes a similar entry route to infect human cells [2].”
Saliva is a non‐negligible factor in the spread of COVID‐19
Li, Y., Ren, B., Peng, X., Hu, T., Li, J., Gong, T., Tang, B., Xu, X., & Zhou, X. (2020) · Molecular Oral Microbiology · doi:10.1111/omi.12289 · Cited by 211
Neurological manifestations of COVID-19: a systematic review and meta-analysis of proportions
Favas, T. T., Dev, P., Chaurasia, R. N., Chakravarty, K., Mishra, R., Joshi, D., Mishra, V. N., Kumar, A., Singh, V. K., Pandey, M., et al. (2020) · Neurological Sciences · doi:10.1007/s10072-020-04801-y · Cited by 218
Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe
Thakur, V., Bhola, S., Thakur, P., Patel, S. K. S., Kulshrestha, S., Ratho, R. K., & Kumar, P. (2022) · Infection · doi:10.1007/s15010-021-01734-2 · Cited by 195
High prevalence of SARS-CoV-2 antibodies in pets from COVID-19+ households
Fritz, M., Rosolen, B., Krafft, É., Becquart, P., Elguero, É., Vratskikh, O., Denolly, S., Boson, B., Vanhomwegen, J., Gouilh, M. A., et al. (2020) · One Health · doi:10.1016/j.onehlt.2020.100192 · Cited by 203
Wu, B., Gu, D.-Z., Yu, J., Yang, J., & Shen, W. (2020) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2020.104485 · Cited by 217
The Immune Response and Immunopathology of COVID-19
Mortaz, E., Tabarsi, P., Varahram, M., Folkerts, G., & Adcock, I. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02037 · Cited by 210
Golden, J. W., Cline, C. R., Zeng, X., Garrison, A. R., Carey, B. D., Mucker, E. M., White, L. E., Shamblin, J. D., Brocato, R. L., Liu, J., et al. (2020) · JCI Insight · doi:10.1172/jci.insight.142032 · Cited by 200
ACE2 binding is an ancestral and evolvable trait of sarbecoviruses
Starr, T. N., Zepeda, S. K., Walls, A. C., Greaney, A. J., Alkhovsky, S. V., Veesler, D., & Bloom, J. D. (2022) · Nature · doi:10.1038/s41586-022-04464-z · Cited by 207
“We also incorporated newly described sarbecovirus sequences RsYN04 17 , PDF-2370 and PRD-0038 14 into updated phylogenies and functional work after the initiation of our study.”
BackgroundHyperglycemia, hydroxychloroquine, and the COVID‐19 pandemic
Brufsky, A. (2020) · Journal of Medical Virology · doi:10.1002/jmv.25887 · Cited by 214
Abdelmageed, M. I., Abdelmoneim, A. H., Mustafa, M. I., Elfadol, N. M., Murshed, N. S., Shantier, S. W., & Makhawi, A. M. (2020) · BioMed Research International · doi:10.1155/2020/2683286 · Cited by 205
“WHO: World Health Organization CoV: Coronaviruses MERS-CoV: Middle East Respiratory Syndrome SARS-CoV: Severe Acute Respiratory Syndrome COVID-19: Novel coronavirus HCoV-HKU1: Human coronavirus HKU1 HCoV-OC43: Human coronavirus OC43 HCoV-NL63: Human coronavirus NL63 HCoV-229E: Human coronavirus 229E ACE2: Angiotensin-…”
BackgroundInfluentialBanu, N., Panikar, S. S., Leal, L. R., & Leal, A. R. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117905 · Cited by 214
Nair, A., Gandhi, R. A., & Natarajan, S. (2020) · Indian Journal of Ophthalmology · doi:10.4103/ijo.ijo_797_20 · Cited by 205
Zhang, Y., Li, H., Zhang, J., Cao, Y., Zhao, X., Yu, N., Gao, Y., Ma, J., Zhang, H., Zhang, J., et al. (2020) · Diabetes Obesity and Metabolism · doi:10.1111/dom.14086 · Cited by 205
On the evolutionary epidemiology of SARS-CoV-2
Day, T., Gandon, S., Lion, S., & Otto, S. P. (2020) · Current Biology · doi:10.1016/j.cub.2020.06.031 · Cited by 208
“R850 Current Biology 30, R841–R870, Augus poor sampling of coronaviruses from wildlife and the wide range of animals with similar ACE2 receptors (including pigs, ferrets, cats, and non-human primates [2]), it is likely that we simply have not identifi ed the most closely related animal source [4], making it impossible…”
Jena, A. B., Kanungo, N., Nayak, V., Chainy, G. B. N., & Dandapat, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-81462-7 · Cited by 208
Heterogeneous expression of the SARS-Coronavirus-2 receptor ACE2 in the human respiratory tract
Ortiz, M. E., Thurman, A. L., Pezzulo, A. A., Leidinger, M., Klesney‐Tait, J., Karp, P. H., Tan, P., Wohlford-Lenane, C., McCray, P. B., & Meyerholz, D. K. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102976 · Cited by 199
“Additionally, compared to SARS-CoV, the SARS-CoV-2 receptor binding motif has a higher affinity for ACE2 [56,57].”
A hypothesis for pathobiology and treatment of COVID‐19 : The centrality of ACE1 / ACE2 imbalance
Sriram, K., & Insel, P. A. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15082 · Cited by 196
“…© 2020 The British Pharmacological Society 4825 range of tissues that are infected, mortality from acute respiratory distress syndrome (ARDS) and their extracellular binding site ACE2 (Wan et al., 2020; Zhang et al., 2020; Zhou, Yang, et al., 2020; Zhou, Yu, et al., 2020).”
BackgroundXu, J., Xu, X., Jiang, L., Dua, K., Hansbro, P. M., & Liu, G. (2020) · Respiratory Research · doi:10.1186/s12931-020-01445-6 · Cited by 199
SARS-CoV-2 Mutations and their Viral Variants
Coşar, B., KARAGÜLLEOĞLU, Z. Y., ÜNAL, S., İnce, A. T., Uncuoglu, D. B., Tuncer, G., Kilinc, B. R., Ozkan, Y. E., Ozkoc, H. C., Demir, I. N., et al. (2021) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2021.06.001 · Cited by 205
“14 high-affinity, computational analyses reveal that the interaction is not so ideal and that the RBD sequence differs from those shown to be optimal for receptor binding in SARS-CoV [49].”
Coronavirus pandemic and colorectal surgery: practical advice based on the Italian experience
di Saverio, S., Pata, F., Gallo, G., Carrano, F., Scorza, A., Sileri, P., Smart, N., Spinelli, A., & Pellino, G. (2020) · Colorectal Disease · doi:10.1111/codi.15056 · Cited by 188
SARS-CoV-2 evolution in an immunocompromised host reveals shared neutralization escape mechanisms
Clark, S. A., Clark, L. E., Pan, J., Coscia, A., McKay, L. G. A., Shankar, S., Johnson, R. I., Brusic, V., Choudhary, M. C., Regan, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.027 · Cited by 193
Hatmal, M. M., Alshaer, W., Al-Hatamleh, M. A. I., Hatmal, M., Smadi, O., Taha, M. O., Oweida, A., Boer, J. C., Mohamud, R., & Plebanski, M. (2020) · Cells · doi:10.3390/cells9122638 · Cited by 205
“In this case, these findings indicate that there are possible differences between the binding residues that are involved in the interactions with the receptor, which, thus, affect binding affinities [1,15,40].”
InfluentialBchetnia, M., Girard, C., Duchaine, C., & Laprise, C. (2020) · Journal of Infection and Public Health · doi:10.1016/j.jiph.2020.07.011 · Cited by 205
Use of mouthwashes against COVID-19 in dentistry
Vergara‐Buenaventura, A., & Castro-Ruiz, C. (2020) · British Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.bjoms.2020.08.016 · Cited by 202
Herbal immune-boosters: Substantial warriors of pandemic Covid-19 battle
Khanna, K., Kohli, S. K., Kaur, R., Bhardwaj, A., Bhardwaj, V., Ohri, P., Sharma, A., Ahmad, A., Bhardwaj, R., & Ahmad, P. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153361 · Cited by 200
SARS-CoV-2 Infects Human Engineered Heart Tissues and Models COVID-19 Myocarditis
Bailey, A. L., Dmytrenko, O., Greenberg, L., Bredemeyer, A. L., Ma, P., Liu, J., Penna, V., Winkler, E. S., Sviben, S., Brooks, E., et al. (2021) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2021.01.002 · Cited by 193
Master Regulator Analysis of the SARS-CoV-2/Human Interactome
Guzzi, P. H., Mercatelli, D., Ceraolo, C., & Giorgi, F. M. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9040982 · Cited by 192
Dhama, K., Patel, S. K., Pathak, M., Yatoo, M. I., Tiwari, R., Malik, Y. S., Singh, R. P., Sah, R., Rabaan, A. A., Bonilla‐Aldana, D. K., et al. (2020) · Travel Medicine and Infectious Disease · doi:10.1016/j.tmaid.2020.101755 · Cited by 196
“S1 subunit of S glycoprotein enables strong binding to the ACE2 receptor while as S2 subunit ensures fusion with the host cell [30,47,113].”
2019 novel coronavirus disease (COVID‐19) in patients with inflammatory bowel diseases
Taxonera, C., Sagastagoitia-Fornie, I., Alba, C., Mañas, N., Olivares, D., & Rey, E. (2020) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.15804 · Cited by 192
One year update on the COVID-19 pandemic: Where are we now?
Mishra, S. K., & Tripathi, T. (2020) · Acta Tropica · doi:10.1016/j.actatropica.2020.105778 · Cited by 196
“in various CoVs, and natural selection has promoted optimal binding affinity during the course of host shifting (Wan et al., 2020; Wrapp et al., 2020; Zhou et al., 2020).”
Peripheral Nervous System Manifestations Associated with COVID-19
Andalib, S., Biller, J., Napoli, M. D., Moghimi, N., McCullough, L. D., Rubiños, C., Nobleza, C. O., Azarpazhooh, M. R., Catanese, L., Elicer, I., et al. (2021) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-021-01102-5 · Cited by 198
COVID-19—Zoonosis or Emerging Infectious Disease?
Haider, N., Rothman-Ostrow, P., Osman, A. Y., Arruda, L. B., Macfarlane-Berry, L., Elton, L., Thomason, M. J., Yeboah‐Manu, D., Ansumana, R., Kapata, N., et al. (2020) · Frontiers in Public Health · doi:10.3389/fpubh.2020.596944 · Cited by 209
“Zoo animals including a tiger and a lion were reported to have been infected by their zoo career (8, 33, 34).”
BackgroundSARS‐CoV‐2, the pandemic coronavirus: Molecular and structural insights
Kadam, S. B., Sukhramani, G. S., Bishnoi, P., Pable, A. A., & Barvkar, V. T. (2021) · Journal of Basic Microbiology · doi:10.1002/jobm.202000537 · Cited by 206
“Therefore, RBD is the critical determinant of virus receptor interaction and reflects host selectivity, virus tropism, and infectivity [88,89].”
BackgroundImmune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Lazarević, I., Pravica, V., Miljanovic, D., & Cupic, M. D. (2021) · Viruses · doi:10.3390/v13071192 · Cited by 193
SARS-CoV-2: The viral shedding vs infectivity dilemma
Widders, A., Broom, A. F., & Broom, J. K. (2020) · Infection Disease & Health · doi:10.1016/j.idh.2020.05.002 · Cited by 189
Molecular Mechanism of Evolution and Human Infection with SARS-CoV-2
He, J., Tao, H., Yan, Y., Huang, S., & Xiao, Y. (2020) · Viruses · doi:10.3390/v12040428 · Cited by 196
Two important controversial risk factors in SARS-CoV-2 infection: Obesity and smoking
Engin, A. B., Engin, A., & Engin, A. (2020) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2020.103411 · Cited by 189
Psycho-Neuroendocrine-Immune Interactions in COVID-19: Potential Impacts on Mental Health
Raony, Í., de Figueiredo, C. S., Pandolfo, P., Giestal-de-Araujo, E., Oliveira-Silva Bomfim, P., & Savino, W. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01170 · Cited by 185
“Although the existence of more than one receptor for this virus cannot be excluded by now, evidence so far reveals that SARS-CoV-2 enters human host cells using the same receptor of SARS-CoV, the human angiotensin-converting enzyme 2 (hACE2) (14).”
BackgroundMinerals and Human Health: From Deficiency to Toxicity
Razzaque, M. S., & Wimalawansa, S. J. (2025) · Nutrients · doi:10.3390/nu17030454 · Cited by 224
“Ca is involved in several pathophysiological aspects of the interaction between SARS-CoV-2 and human host cells [54,55].”
Viana, S., Nunes, S., & Reis, F. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101123 · Cited by 185
Shahriarirad, R., Khodamoradi, Z., Erfani, A., Hosseinpour, H., Ranjbar, K., Emami, Y., Mirahmadizadeh, A., Lotfi, M., Yeganeh, B. S., Nejad, A. D., et al. (2020) · BMC Infectious Diseases · doi:10.1186/s12879-020-05128-x · Cited by 178
I mmunosenescence and Inflammaging: Risk Factors of Severe COVID-19 in Older People
Pietrobon, A. J., Teixeira, F. M. E., & Sato, M. N. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.579220 · Cited by 187
Revealing the Potency of Citrus and Galangal Constituents to Halt SARS-CoV-2 InfectionPreprint
Utomo, R. Y., Ikawati, M., & Meiyanto, E. (2020) · Preprints.org · doi:10.20944/preprints202003.0214.v1 · Cited by 184
Magrone, T., Magrone, M., & Jirillo, E. (2020) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530320666200427112902 · Cited by 186
Potential Applications of Plant Biotechnology against SARS-CoV-2
Capell, T., Twyman, R. M., Armario-Nájera, V., K‐C., J., Schillberg, S., & Christou, P. (2020) · Trends in Plant Science · doi:10.1016/j.tplants.2020.04.009 · Cited by 185
Davidson, A. M., Wysocki, J. A., & BATLLE, D. C. (2020) · Hypertension · doi:10.1161/hypertensionaha.120.15256 · Cited by 183
“In the current pandemic, ACE2 was predicted in January 2020 to be the receptor for SARS-CoV-2 by Wan et al(11) by comparing previous SARS-CoV structural analyses of atomic-level interactions between the RBD and ACE2 with the newly released genetic sequence of SARS-CoV-2.(11) Then in early February, virus infectivity s…”
InfluentialRobson, B. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.103749 · Cited by 185
Evaluation of K18-hACE2 Mice as a Model of SARS-CoV-2 Infection
Moreau, G. B., Burgess, S. L., Sturek, J. M., Donlan, A. N., Petri, W. A., & Mann, B. J. (2020) · American Journal of Tropical Medicine and Hygiene · doi:10.4269/ajtmh.20-0762 · Cited by 181
COVID-19 and SARS-Cov-2 Infection: Pathophysiology and Clinical Effects on the Nervous System
Abboud, H., Abboud, F. Z., Kharbouch, H., Arkha, Y., Abbadi, N. E., & Ouahabi, A. E. (2020) · World Neurosurgery · doi:10.1016/j.wneu.2020.05.193 · Cited by 177
“Genomicanalysis shows thatSARS-CoV-2 is in the same beta-coronavirus clade as MERS-CoV and SARS-CoV and shares a highly homologic sequence with SARS-CoV.”
BackgroundInfluentialEicosanoid signalling blockade protects middle-aged mice from severe COVID-19
Wong, L.-Y. R., Zheng, J., Wilhelmsen, K., Li, K., Ortiz, M. E., Schnicker, N. J., Thurman, A., Pezzulo, A. A., Szachowicz, P. J., Li, P., et al. (2022) · Nature · doi:10.1038/s41586-022-04630-3 · Cited by 178
Severe COVID‐19 infection and thrombotic microangiopathy: success does not come easily
Gavriilaki, E., & Brodsky, R. A. (2020) · British Journal of Haematology · doi:10.1111/bjh.16783 · Cited by 178
“Similarly, ACE2 is highly expressed on podocytes and tubule epithelial cells of the kidney, whereas a recent study has suggested viral tropism for the kidney.(8) Furthermore, studies of previous coronaviruses have shown that blocking C3 activation significantly attenuates the lungdirected proinflammatory sequelae of i…”
BackgroundCOVID-19 and Respiratory System Disorders
Brosnahan, S. B., Jonkman, A. H., Kugler, M. C., Munger, J. S., & Kaufman, D. A. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.314515 · Cited by 182
Triggle, C. R., Bansal, D., Ding, H., Islam, M. M., Farag, E., Hadi, H. A., & Sultan, A. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.631139 · Cited by 187
Immunology of SARS-CoV-2 infection in children
Chou, J. S., Thomas, P. G., & Randolph, A. G. (2022) · Nature Immunology · doi:10.1038/s41590-021-01123-9 · Cited by 176
Bioactive natural compounds against human coronaviruses: a review and perspective
Xian, Y., Zhang, J., Bian, Z., Zhou, H., Zhang, Z., Lin, Z., & Xu, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.06.002 · Cited by 183
Predictors for Severe COVID-19 Infection
Bhargava, A., Fukushima, E. A., Levine, M. T., Zhao, W., Tanveer, F., Szpunar, S. M., & Saravolatz, L. D. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa674 · Cited by 176
“SARS-CoV-2 is strongly suspected to use ACE2 as its receptor, and ACE2 binding affinity has been shown to be one of the most important determinants of SARS-CoV infectivity [28].”
BackgroundNatural Killer Cell Dysfunction and Its Role in COVID-19
van Eeden, C., Khan, L., Osman, M. S., & Tervaert, J. W. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176351 · Cited by 179
“SARS-CoV-2 has also been shown to utilize ACE2 as a cell entry receptor [89,90], intriguingly ACE2 activity is increased in both pulmonary and cardiovascular disease [91,92].”
BackgroundAnimal models of mechanisms of SARS‐CoV‐2 infection and COVID‐19 pathology
Cleary, S. J., Pitchford, S. C., Amison, R. T., Carrington, R., Cabrera, C. L. R., Magnen, M., Looney, M. R., Gray, E., & Page, C. P. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15143 · Cited by 169
“Mouse adaptation of SARS-CoV-2 would be useful for the acceleration of mouse testing but may prove difficult as SARS-CoV-2 Spike appears to have evolved high affinity for human ACE2 at the expense of lower affinity for ACE2 in other organisms (Wan et al., 2020).”
BackgroundPulmonary and Extra-Pulmonary Clinical Manifestations of COVID-19
Johnson, K. D., Harris, C. C., Cain, J., Hummer, C., Goyal, H., & Perisetti, A. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00526 · Cited by 185
“Additionally, studies have found overexpression of ACE-2 in the epithelial cells of the GI tract, suggesting SARS-CoV-2 replication in the GI tract (42).”
BackgroundAnimal and translational models of SARS-CoV-2 infection and COVID-19
Johansen, M. D., Irving, A. T., Montagutelli, X., Tate, M. D., Rudloff, I., Nold, M. F., Hansbro, N. G., Kim, R., Donovan, C., Liu, G., et al. (2020) · Mucosal Immunology · doi:10.1038/s41385-020-00340-z · Cited by 173
“115 117 Recently, ferret ACE2 was shown to contain the critical residues required for binding by SARS-CoV-2 RBD. 118 The animals were susceptible to SARS-CoV-2 infection with viral replication in the URT, however, only low levels of virus were detected in lungs.”
Background
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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