SARS-CoV-2 growth, furin-cleavage-site adaptation and neutralization using serum from acutely infected hospitalized COVID-19 patients
Open accessPublished version of a preprint
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of coronavirus disease 2019 (COVID-19), emerged at the end of 2019 and by mid-June 2020 the virus had spread to at least 215 countries, caused more than 8 000 000 confirmed infections and over 450 000 deaths, and overwhelmed healthcare systems worldwide. Like severe acute respiratory syndrome coronavirus (SARS-CoV), which emerged in 2002 and caused a similar disease, SARS-CoV-2 is a betacoronavirus. Both viruses use human angiotensin-converting enzyme 2 (hACE2) as a receptor to enter cells. However, the SARS-CoV-2 spike (S) glycoprotein has a novel insertion that generates a putative furin cleavage signal and this has been postulated to expand the host range. Two low-passage (P) strains of SARS-CoV-2 (Wash1 : P4 and Munich : P1) were cultured twice in Vero E6 cells and characterized virologically. Sanger and MinION sequencing demonstrated significant deletions in the furin cleavage signal of Wash1 : P6 and minor variants in the Munich : P3 strain. Cleavage of the S glycoprotein in SARS-CoV-2-infected Vero E6 cell lysates was inefficient even when an intact furin cleavage signal was present. Indirect immunofluorescence demonstrated that the S glycoprotein reached the cell surface. Since the S protein is a major antigenic target for the development of neutralizing antibodies, we investigated the development of neutralizing antibody titres in serial serum samples obtained from COVID-19 human patients. These were comparable regardless of the presence of an intact or deleted furin cleavage signal. These studies illustrate the need to characterize virus stocks meticulously prior to performing either in vitro or in vivo pathogenesis studies.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Propagation in Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells prevented adventitious spike mutations, especially near furin cleavage site.
“Recombinant viruses and B.1.1.7 were propagated in Vero-TMPRSS2 and Vero-hACE2-TMPRSS2 cells expressing transmembrane protease serine 2 (TMPRSS2) and human angiotensin converting enzyme 2 (hACE2) to prevent the development of adventitious mutations in the spike, especially at or near the furin cleavage site”
From Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies (2021) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
A novel coronavirus from patients with pneumonia in China, 2019
Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., Zhao, X., Huang, B., Shi, W., Lu, R., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2001017 · Cited by 28,244 · see citing works
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 · see citing works
Hoffmann, 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 · see citing works
Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
Walls, A. C., Park, Y.-J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020) · doi:10.1101/2020.02.19.956581 · Cited by 8,586 · see citing works
Gorbalenya, 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 8,436 · see citing works
Virological assessment of hospitalized patients with COVID-2019
Wölfel, R., Corman, V. M., Guggemos, W., Seilmaier, M., Zange, S., Müller, M. A., Niemeyer, D., Jones, T. C., Vollmar, P., Rothe, C., et al. (2020) · Nature · doi:10.1038/s41586-020-2196-x · Cited by 6,661 · see citing works
Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia
Zaki, A. M., van Boheemen, S., Bestebroer, T. M., Osterhaus, A. D. M. E., & Fouchier, R. A. M. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1211721 · Cited by 5,677 · see citing works
The proximal origin of SARS-CoV-2
Andersen, K. G., Rambaut, A., Lipkin, W. I., Holmes, E. C., & Garry, R. F. (2020) · Nature Medicine · doi:10.1038/s41591-020-0820-9 · Cited by 5,081 · see citing works
Identification of a novel coronavirus in patients with severe acute respiratory syndrome
Drosten, C., Günther, S., Preiser, W., van der Werf, S., Brodt, H.-R., Becker, S., Rabenau, H., Panning, M., Kolesnikova, L., Fouchier, R. A. M., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030747 · Cited by 4,574 · see citing works
A Novel Coronavirus Associated with Severe Acute Respiratory Syndrome
Tg, K., Erdman, D. D., Cs, G., Zaki, Peret, T. C. T., Emery, S. L., Tong, S., Urbani, C., Comer, J. A., Lim, W., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030781 · Cited by 4,345 · see citing works
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281 · see citing works
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · see citing works
Grifoni, A., Weiskopf, D., Ramirez, S. I., Mateus, J., Dan, J. M., Moderbacher, C. R., Rawlings, S. A., Sutherland, A., Premkumar, L., Jadi, R. S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.015 · Cited by 3,595 · see citing works
Cell entry mechanisms of SARS-CoV-2
Shang, J., Wan, Y., Luo, C., Ye, G., Geng, Q., Auerbach, A., & Li, F. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003138117 · Cited by 3,142 · see citing works
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · see citing works
Ou, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097 · see citing works
To, K. K., Tsang, O. T.-Y., Leung, W.-S., Tam, A. R., Wu, T.-C., Lung, D. C., Yip, C. C., Cai, J., Chan, J. M., Chik, T. S., et al. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30196-1 · Cited by 3,045 · see citing works
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 · see citing works
Opportunities and challenges in long-read sequencing data analysis
Amarasinghe, S. L., Su, S., Dong, X., Zappia, L., Ritchie, M. E., & Gouil, Q. (2020) · Genome Biology · doi:10.1186/s13059-020-1935-5 · Cited by 2,530 · see citing works
Hoffmann, M., Kleine-Weber, H., & Pöhlmann, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.022 · Cited by 1,852 · see citing works
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
Ge, X.-Y., Li, J.-L., Yang, X.-L., Chmura, A. A., Zhu, G., Epstein, J. H., Mazet, J. K., Hu, B., Zhang, W., Peng, C., et al. (2013) · Nature · doi:10.1038/nature12711 · Cited by 1,778 · see citing works
Coutard, B., Valle, C., de Lamballerie, X. N., Canard, B., Seidah, N. G., & Decroly, É. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104742 · Cited by 1,685 · see citing works
Okba, N. M. A., Müller, M. A., Li, W., Wang, C., GeurtsvanKessel, C. H., Corman, V. M., Lamers, M. M., Sikkema, R. S., de Bruin, E., Chandler, F. D., et al. (2020) · Emerging Infectious Diseases · doi:10.3201/eid2607.200841 · Cited by 1,614 · see citing works
Profiling Early Humoral Response to Diagnose Novel Coronavirus Disease (COVID-19)
Guo, L., Ren, L., Yang, S., Xiao, M., Chang, D., Yang, F., Cruz, C. S. D., Wang, Y., Wu, C., Xiao, Y., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa310 · Cited by 1,585 · see citing works
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489 · see citing works
SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity
Zhang, L., Jackson, C. B., Mou, H., Ojha, A., Peng, H., Quinlan, B. D., Rangarajan, E. S., Pan, A., Vanderheiden, A., Suthar, M. S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19808-4 · Cited by 1,387 · see citing works
Belouzard, S., Chu, V. C., & Whittaker, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809524106 · Cited by 1,073 · see citing works
The Coronavirus Nucleocapsid Is a Multifunctional Protein
McBride, R., van Zyl, M., & Fielding, B. C. (2014) · Viruses · doi:10.3390/v6082991 · Cited by 928 · see citing works
Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis
Millet, J. K., & Whittaker, G. R. (2014) · Virus Research · doi:10.1016/j.virusres.2014.11.021 · Cited by 887 · see citing works
Wu, F., Wang, A., Liu, M., Wang, Q., Chen, J., Xia, S., Ling, Y., Zhang, Y., Xun, J., Lu, L., et al. (2020) · doi:10.1101/2020.03.30.20047365 · Cited by 754 · see citing works
The D614G mutation in the SARS-CoV-2 spike protein reduces S1 shedding and increases infectivityPreprint
Zhang, L., Jackson, C. B., Mou, H., et al. (2020) · bioRxiv · doi:10.1101/2020.06.12.148726 · Cited by 576 · see citing works
Severe Acute Respiratory Syndrome Coronavirus 2 from Patient with Coronavirus Disease, United States
Harcourt, J. L., Tamin, A., Lu, X., Kamili, S., Sakthivel, S. K., Murray, J., Queen, K. J., Tao, Y., Paden, C. R., Zhang, J., et al. (2020) · Emerging infectious diseases · doi:10.3201/eid2606.200516 · Cited by 524 · see citing works
Ogando, N. S., Dalebout, T. J., Zevenhoven-Dobbe, J. C., Limpens, R. W. A. L., van der Meer, Y., Caly, L., Druce, J. D., de Vries, J. J. C., Kikkert, M., Bárcena, M., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001453 · Cited by 524 · see citing works
Siu, Y. L., Teoh, K.-T., Lo, J., Chan, C. M., Kien, F., Escriou, N., Tsao, S. W., Nicholls, J. M., Altmeyer, R. M., Peiris, M. J. S., et al. (2008) · Journal of Virology · doi:10.1128/jvi.01052-08 · Cited by 503 · see citing works
Davidson, A. D., Williamson, M. K., Lewis, S., Shoemark, D., Carroll, M. W., Heesom, K. J., Zambon, M., Ellis, J., Lewis, P. A., Hiscox, J. A., et al. (2020) · Genome Medicine · doi:10.1186/s13073-020-00763-0 · Cited by 457 · see citing works
Patel, A., Jernigan, D. B., 2019-nCoV CDC Response Team, 2019-nCoV CDC Response Team, Abdirizak, F., Abedi, G. R., Aggarwal, S., Albina, D., Allen, E., Andersen, L., et al. (2020) · MMWR Morbidity and Mortality Weekly Report · doi:10.15585/mmwr.mm6905e1 · Cited by 446 · see citing works
Case, J. B., Rothlauf, P. W., Chen, R. E., Liu, Z., Zhao, H., Kim, A. S., Bloyet, L.-M., Zeng, Q., Tahan, S., Droit, L., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.021 · Cited by 410 · see citing works
Cross-reactive Antibody Response between SARS-CoV-2 and SARS-CoV Infections
Lv, H., Wu, N. C., Tsang, O. T.-Y., Yuan, M., Perera, R. A. P. M., Leung, W.-S., So, R. T. Y., Chan, J. M. C., Yip, G. K., Chik, T. S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107725 · Cited by 401 · see citing works
Coronavirus Cell Entry Occurs through the Endo-/Lysosomal Pathway in a Proteolysis-Dependent Manner
Tait‐Burkard, C., Verheije, M. H., Wicht, O., van Kasteren, S. I., van Kuppeveld, F. J. M., Haagmans, B. L., Pelkmans, L., Rottier, P. J. M., Bosch, B., & de Haan, C. A. M. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004502 · Cited by 389 · see citing works
Close Relative of Human Middle East Respiratory Syndrome Coronavirus in Bat, South Africa
Ithete, N. L., Stoffberg, S., Corman, V. M., Cottontail, V. M., Richards, L. R., Schoeman, M. C., Drosten, C., Drexler, J. F., & Preiser, W. (2013) · Emerging infectious diseases · doi:10.3201/eid1910.130946 · Cited by 381 · see citing works
Klimstra, W. B., Ryman, K. D., & Johnston, R. E. (1998) · Journal of Virology · doi:10.1128/jvi.72.9.7357-7366.1998 · Cited by 381 · see citing works
Self-citationPoh, C. M., Carissimo, G., Wang, B., Amrun, S. N., Lee, C. Y., Chee, R. S., Fong, S., Yeo, N. K., Lee, W.-H., Torres‐Ruesta, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16638-2 · Cited by 379 · see citing works
Ready, Set, Fuse! The Coronavirus Spike Protein and Acquisition of Fusion Competence
Heald-Sargent, T. A., & Gallagher, T. (2012) · Viruses · doi:10.3390/v4040557 · Cited by 322 · see citing works
Serological assays for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), March 2020
Perera, R. A. P. M., Mok, C. K. P., Tsang, O. T., Lv, H., Ko, R. L., Wu, N. C., Yuan, M., Leung, W.-S., Chan, J. M., Chik, T. S., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.16.2000421 · Cited by 322 · see citing works
Attenuated SARS-CoV-2 variants with deletions at the S1/S2 junction
Lau, S.-Y., Wang, P., Mok, B. W.-Y., Zhang, J., Chu, H., Lee, A. C.-Y., Deng, S., Chen, P., Chan, K., Song, W., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1756700 · Cited by 291 · see citing works
Viruses in bats and potential spillover to animals and humans
Wang, L., & Anderson, D. E. (2019) · Current Opinion in Virology · doi:10.1016/j.coviro.2018.12.007 · Cited by 285 · see citing works
Soneson, C., Yao, Y., Bratus-Neuenschwander, A., Patrignani, A., Robinson, M. D., & Hussain, S. (2019) · Nature Communications · doi:10.1038/s41467-019-11272-z · Cited by 257 · see citing works
Haveri, A., Smura, T., Kuivanen, S. H., Österlund, P., Hepojoki, J., Ikonen, N., Pitkäpaasi, M., Blomqvist, S., Rönkkö, E., Kantele, A., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.11.2000266 · Cited by 255 · see citing works
Membrane Binding Proteins of Coronaviruses
Alsaadi, E. A. J., & Jones, I. M. (2019) · Future Virology · doi:10.2217/fvl-2018-0144 · Cited by 226 · see citing works
Bernard, K. A., Klimstra, W. B., & Johnston, R. E. (2000) · Virology · doi:10.1006/viro.2000.0546 · Cited by 223 · see citing works
Self-citationEmergence of Drift Variants That May Affect COVID-19 Vaccine Development and Antibody Treatment
Koyama, T., Weeraratne, D., Snowdon, J. L., & Parida, L. (2020) · Pathogens · doi:10.3390/pathogens9050324 · Cited by 223 · see citing works
TMPRSS2 and TMPRSS4 Facilitate Trypsin-Independent Spread of Influenza Virus in Caco-2 Cells
Bertram, S., Glowacka, I., Błażejewska, P., Soilleux, E. J., Allen, P., Danisch, S., Steffen, I., Choi, S.-Y., Park, Y., Schneider, H., et al. (2010) · Journal of Virology · doi:10.1128/jvi.00239-10 · Cited by 196 · see citing works
Case, J., Rothlauf, P. W., Chen, R. E., et al. (2020) · bioRxiv · doi:10.1101/2020.05.18.102038 · Cited by 162 · see citing works
Liu, Z., Zheng, H., Lin, H., Li, M., Yuan, R., Peng, J., Xiong, Q., Sun, J., Li, B., Wu, J., et al. (2020) · Journal of Virology · doi:10.1128/jvi.00790-20 · Cited by 162 · see citing works
Hartman, A. L., Nambulli, S., McMillen, C. M., White, A. G., Tilston‐Lunel, N. L., Albe, J. R., Cottle, E. L., Dunn, M., Frye, L. J., Gilliland, T. H., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008903 · Cited by 136 · see citing works
Self-citationHigh neutralizing antibody titer in intensive care unit patients with COVID-19
Liu, L., To, K. K., Chan, K., Wong, M. Y.-C., Zhou, R., Kwan, K., Fong, C. H.-Y., Chen, L., Choi, C. Y.-K., Lu, L., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1791738 · Cited by 132 · see citing works
Cross-reactive antibody response between SARS-CoV-2 and SARS-CoV infectionsPreprint
Lv, H., Wu, N. C., Tsang, O. T., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.15.993097 · Cited by 101 · see citing works
Infection of Neonatal Mice with Sindbis Virus Results in a Systemic Inflammatory Response Syndrome
Klimstra, W. B., Ryman, K. D., Bernard, K. A., Nguyen, K. B., Biron, C. A., & Johnston, R. E. (1999) · Journal of Virology · doi:10.1128/jvi.73.12.10387-10398.1999 · Cited by 95 · see citing works
Self-citationLack of cross-neutralization by SARS patient sera towards SARS-CoV-2
Anderson, D. E., Tan, C. W., Chia, W. N., Young, B. E., Linster, M., Low, J. G. H., Tan, Y., Chen, M. I.-C., Smith, G. J. D., Leo, Y., et al. (2020) · Emerging Microbes & Infections · doi:10.1080/22221751.2020.1761267 · Cited by 94 · see citing works
Gardner, C. L., Hritz, J., Sun, C., Vanlandingham, D. L., Song, T., Ghedin, E., Higgs, S., Klimstra, W. B., & Ryman, K. D. (2014) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0002719 · Cited by 92 · see citing works
Self-citationSmit, J. M., Waarts, B.-L., Kimata, K., Klimstra, W. B., Bittman, R., & Wilschut, J. (2002) · Journal of Virology · doi:10.1128/jvi.76.20.10128-10137.2002 · Cited by 88 · see citing works
Self-citationRyman, K. D., Gardner, C. L., Burke, C. W., Meier, K. C., Thompson, J. M., & Klimstra, W. B. (2007) · Journal of Virology · doi:10.1128/jvi.02494-06 · Cited by 79 · see citing works
Self-citationParticle-to-PFU Ratio of Ebola Virus Influences Disease Course and Survival in Cynomolgus Macaques
Alfson, K. J., Avena, L. E., Beadles, M. W., Staples, H. M., Nunneley, J. W., Ticer, A. E., Dick, E. J., Owston, M. A., Reed, C. D., Patterson, J. L., et al. (2015) · Journal of Virology · doi:10.1128/jvi.00649-15 · Cited by 69 · see citing works
Davidson, A. D., Williamson, M. K., Lewis, S., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.22.002204 · Cited by 62 · see citing works
Kim, S. J., Nguyen, V. G., Park, Y., Park, B., & Chung, H. (2020) · Vaccines · doi:10.3390/vaccines8020220 · Cited by 55 · see citing works
Hartman, A. L., Nambulli, S., McMillen, C. M., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.20.137687 · Cited by 42 · see citing works
Self-citationHeidner, H. W., McKnight, K. L., Davis, N., & Johnston, R. E. (1994) · Journal of Virology · doi:10.1128/jvi.68.4.2683-2692.1994 · Cited by 41 · see citing works
Oliva, R., Shaikh, A. R., Petta, A., Vangone, A., & Cavallo, L. (2021) · Molecules · doi:10.3390/molecules26092622 · Cited by 39 · see citing works
Cavallo, L., & Oliva, R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.08.140152 · Cited by 16 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Grifoni, A., Weiskopf, D., Ramirez, S. I., Mateus, J., Dan, J. M., Moderbacher, C. R., Rawlings, S. A., Sutherland, A., Premkumar, L., Jadi, R. S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.015 · Cited by 3,595 · see citing works
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,082 · see citing works
Opportunities and challenges in long-read sequencing data analysis
Amarasinghe, S. L., Su, S., Dong, X., Zappia, L., Ritchie, M. E., & Gouil, Q. (2020) · Genome Biology · doi:10.1186/s13059-020-1935-5 · Cited by 2,530 · see citing works
Lamers, M. M., & Haagmans, B. L. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00713-0 · Cited by 986 · see citing works
Chen, R. E., Zhang, X., Case, J. B., Winkler, E. S., Liu, Y., VanBlargan, L. A., Liu, J., Errico, J. M., Xie, X., Suryadevara, N., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01294-w · Cited by 881 · see citing works
The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets
Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., Kugathasan, R., Penn, R., Brown, J. C., Sanchez-David, R. Y., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00908-w · Cited by 770 · see citing works
Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis
Johnson, B. A., Xie, X., Bailey, A. L., Kalveram, B., Lokugamage, K. G., Muruato, A., Zou, J., Zhang, X., Juelich, T., Smith, J. K., et al. (2021) · Nature · doi:10.1038/s41586-021-03237-4 · Cited by 694 · see citing works
Deng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · doi:10.1101/2021.03.07.21252647 · Cited by 651 · see citing works
Transmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant
Deng, X., Garcia-Knight, M. A., Khalid, M. M., Servellita, V., Wang, C., Morris, M. K., Sotomayor-González, A., Glasner, D. R., Reyes, K. R., Gliwa, A. S., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.025 · Cited by 651 · see citing works
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Network for Genomic Surveillance in South Africa, Cele, S., COMMIT-KZN Team, Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03471-w · Cited by 651 · see citing works
Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape
McCarthy, K. R., Rennick, L. J., Nambulli, S., Robinson-McCarthy, L. R., Bain, W. G., Haidar, G., & Duprex, W. P. (2021) · Science · doi:10.1126/science.abf6950 · Cited by 535 · see citing works
Self-citationThe origins of SARS-CoV-2: A critical review
Holmes, E. C., Goldstein, S. A., Rasmussen, A. L., Robertson, D. L., Crits‐Christoph, A., Wertheim, J. O., Anthony, S. J., Barclay, W., Boni, M. F., Doherty, P. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.08.017 · Cited by 510 · see citing works
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman‐Duhovny, D., Zhang, C., & Shi, Y. (2020) · Science · doi:10.1126/science.abe4747 · Cited by 394 · see citing works
Self-citationAntibody response to SARS-CoV-2 infection in humans: A systematic review
Post, N., Eddy, D., Huntley, C., van Schalkwyk, M. C., Shrotri, M., Leeman, D., Rigby, S., Williams, S. V., Bermingham, W. H., Kellam, P., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0244126 · Cited by 367 · see citing works
T cell response to SARS-CoV-2 infection in humans: A systematic review
Shrotri, M., van Schalkwyk, M. C., Post, N., Eddy, D., Huntley, C., Leeman, D., Rigby, S., Williams, S. V., Bermingham, W. H., Kellam, P., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0245532 · Cited by 349 · see citing works
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285 · see citing works
Rihn, S. J., Merits, A., Bakshi, S., Turnbull, M. L., Wickenhagen, A., Alexander, A. J. T., Baillie, C., Brennan, B., Brown, F., Brunker, K., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001091 · Cited by 204 · see citing works
In vivo monoclonal antibody efficacy against SARS-CoV-2 variant strains
Chen, R. E., Winkler, E. S., Case, J. B., Aziati, I. D., Bricker, T. L., Joshi, A., Darling, T. L., Ying, B., Errico, J. M., Shrihari, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03720-y · Cited by 209 · see citing works
Proteolytic activation of SARS‐CoV‐2 spike protein
Takeda, M. (2021) · Microbiology and Immunology · doi:10.1111/1348-0421.12945 · Cited by 182 · see citing works
Sasaki, M., Uemura, K., Sato, A., Toba, S., Sanaki, T., Maenaka, K., Hall, W. W., Orba, Y., & Sawa, H. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009233 · Cited by 179 · see citing works
In vitro selection of Remdesivir resistance suggests evolutionary predictability of SARS-CoV-2
Szemiel, A. M., Merits, A., Orton, R. J., MacLean, O. A., Pinto, R. M., Wickenhagen, A., Lieber, G., Turnbull, M. L., Wang, S., Furnon, W., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009929 · Cited by 175 · see citing works
Nambulli, S., Xiang, Y., Tilston-Lunel, N. L., Rennick, L., Sang, Z., Klimstra, W., Reed, D., Crossland, N., Shi, Y., & Duprex, W. P. (2021) · Science Advances · doi:10.1126/sciadv.abh0319 · Cited by 135 · see citing works
Self-citationA versatile reverse genetics platform for SARS-CoV-2 and other positive-strand RNA viruses
Amarilla, A. A., Sng, J. D. J., Parry, R. H., Deerain, J. M., Potter, J. R., Setoh, Y. X., Rawle, D. J., Le, T. T., Modhiran, N., Wang, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23779-5 · Cited by 158 · see citing works
SARS-CoV-2 one year on: evidence for ongoing viral adaptation
Peacock, T. P., Penrice-Randal, R., Hiscox, J. A., & Barclay, W. (2021) · Journal of General Virology · doi:10.1099/jgv.0.001584 · Cited by 149 · see citing works
Mykytyn, A. Z., Breugem, T. I., Riesebosch, S., Schipper, D., van den Doel, P. B., Rottier, R. J., Lamers, M. M., & Haagmans, B. L. (2021) · eLife · doi:10.7554/elife.64508 · Cited by 150 · see citing works
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Cele, S., Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., Wilkinson, E., Naidoo, Y., et al. (2021) · doi:10.1101/2021.01.26.21250224 · Cited by 651 · see citing works
Hartman, A. L., Nambulli, S., McMillen, C. M., White, A. G., Tilston‐Lunel, N. L., Albe, J. R., Cottle, E. L., Dunn, M., Frye, L. J., Gilliland, T. H., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008903 · Cited by 136 · see citing works
Self-citationCOVID-19 in Relation to Hyperglycemia and Diabetes Mellitus
Al-Kuraishy, H. M., Al-Gareeb, A. I., Alblihed, M. A., Guerreiro, S. G., Martins, N. A., & Batiha, G. E. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.644095 · Cited by 130 · see citing works
Laporte, M., Raeymaekers, V., Berwaer, R. V., Vandeput, J., Marchand-Casas, I., Thibaut, H. J., Looveren, D. V., Martens, K., Hoffmann, M., Maes, P., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009500 · Cited by 123 · see citing works
Synergistic and Antagonistic Drug Combinations against SARS-CoV-2
Bobrowski, T., Chen, L., Eastman, R. T., Itkin, Z., Shinn, P., Chen, C. Z., Guo, H., Zheng, W., Michael, S., Simeonov, A. M., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.12.016 · Cited by 112 · see citing works
Replication kinetics and infectivity of SARS-CoV-2 variants of concern in common cell culture models
Mautner, L., Hoyos, M., Dangel, A., Berger, C., Ehrhardt, A., & Baiker, A. E. (2022) · Virology Journal · doi:10.1186/s12985-022-01802-5 · Cited by 104 · see citing works
Beumer, J., Geurts, M. H., Lamers, M. M., Puschhof, J., Zhang, J., van der Vaart, J., Mykytyn, A. Z., Breugem, T. I., Riesebosch, S., Schipper, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25729-7 · Cited by 107 · see citing works
Human airway cells prevent SARS-CoV-2 multibasic cleavage site cell culture adaptation
Lamers, M. M., Mykytyn, A. Z., Breugem, T. I., Wang, Y., Wu, D. C., Riesebosch, S., van den Doel, P. B., Schipper, D., Bestebroer, T. M., Wu, N. C., et al. (2021) · eLife · doi:10.7554/elife.66815 · Cited by 100 · see citing works
Functional importance of the D614G mutation in the SARS-CoV-2 spike protein
Jackson, C. B., Zhang, L., Farzan, M., & Choe, H. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.11.026 · Cited by 90 · see citing works
The origins of COVID‐19 pandemic: A brief overview
Hao, Y., Wang, Y., Wang, M.-Y., Zhou, L., Shi, J., Cao, J., & Wang, D. (2022) · Transboundary and Emerging Diseases · doi:10.1111/tbed.14732 · Cited by 103 · see citing works
Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., Kugathasan, R., Penn, R., Brown, J. C., Sanchez-David, R. Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.318311 · Cited by 88 · see citing works
Rosa, R. B., Dantas, W. M., do Nascimento, J. C. F., da Silva, M. V., de Oliveira, R. N., & Pena, L. (2021) · Viruses · doi:10.3390/v13030379 · Cited by 84 · see citing works
Ramírez, S., Fernandez-Antunez, C., Galli, A., Underwood, A. P., Pham, L. V., Ryberg, L. A., Feng, S., Pedersen, M. S., Mikkelsen, L. S., Belouzard, S., et al. (2021) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00097-21 · Cited by 87 · see citing works
Zhang, X., Liu, Y., Liu, J., Bailey, A. L., Plante, K. S., Plante, J. A., Zou, J., Xia, H., Bopp, N. E., Aguilar, P. V., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.044 · Cited by 80 · see citing works
Despres, H. W., Mills, M. G., Shirley, D. J., Schmidt, M. M., Huang, M.-L. W., Roychoudhury, P., Jerome, K. R., Greninger, A. L., & Bruce, E. A. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2116518119 · Cited by 70 · see citing works
SARS-CoV-2 variants reveal features critical for replication in primary human cells
Pohl, M. O., Busnadiego, I., Kufner, V., Glas, I., Karakus, U., Schmutz, S., Zaheri, M., Abela, I. A., Trkola, A., Huber, M., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001006 · Cited by 54 · see citing works
Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · doi:10.1101/2021.01.27.428529 · Cited by 55 · see citing works
Virus-like Particles: Measures and Biological Functions
Bhat, T., Cao, A., & Yin, J. (2022) · Viruses · doi:10.3390/v14020383 · Cited by 53 · see citing works
Advancing lung organoids for COVID-19 research
van der Vaart, J., Lamers, M. M., Haagmans, B. L., & Clevers, H. C. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.049060 · Cited by 50 · see citing works
Furusawa, Y., Kiso, M., Iida, S., Uraki, R., Hirata, Y., Imai, M., Suzuki, T., Yamayoshi, S., & Kawaoka, Y. (2023) · EBioMedicine · doi:10.1016/j.ebiom.2023.104561 · Cited by 46 · see citing works
Sasaki, M., Toba, S., Itakura, Y., Chambaro, H. M., Kishimoto, M., Tabata, K., Intaruck, K., Uemura, K., Sanaki, T., Sato, A., et al. (2021) · mBio · doi:10.1128/mbio.01415-21 · Cited by 44 · see citing works
Lavie, M., Dubuisson, J., & Belouzard, S. (2022) · Journal of Virology · doi:10.1128/jvi.00474-22 · Cited by 48 · see citing works
McCormick, W. L., & Mermel, L. A. (2021) · Virology Journal · doi:10.1186/s12985-021-01566-4 · Cited by 46 · see citing works
Shiliaev, N., Lukash, T., Palchevska, O., Crossman, D. K., Green, T. J., Crowley, M. R., Frolova, E. I., & Frolov, I. V. (2021) · Journal of Virology · doi:10.1128/jvi.01357-21 · Cited by 40 · see citing works
Yun, S., Ryu, J. H., Jang, J. H., Bae, H., Yoo, S.-H., Choi, A., Jo, S. J., Lim, J., Lee, J., Ryu, H., et al. (2021) · Annals of Laboratory Medicine · doi:10.3343/alm.2021.41.6.577 · Cited by 39 · see citing works
Chen, R. E., Gorman, M. J., Zhu, D. Y., Carreño, J. M., Yuan, D., VanBlargan, L. A., Burdess, S., Lauffenburger, D. A., Kim, W., Turner, J. S., et al. (2021) · Med · doi:10.1016/j.medj.2021.11.004 · Cited by 36 · see citing works
Propagation of SARS-CoV-2 in Calu-3 Cells to Eliminate Mutations in the Furin Cleavage Site of Spike
Baczenas, J. J., Andersen, H., Rashid, S., Yarmosh, D. A., Puthuveetil, N. P., Parker, M. L., Bradford, R., Florence, C., Stemple, K. J., Lewis, M. G., et al. (2021) · Viruses · doi:10.3390/v13122434 · Cited by 37 · see citing works
Structural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2
Gupta, K., Toelzer, C., Williamson, M. K., Shoemark, D. K., Oliveira, A. S. F., Matthews, D. A., Almuqrin, A., Staufer, O., Yadav, S. K. N., Borucu, U., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27881-6 · Cited by 36 · see citing works
Garg, A., Hawks, S. A., Pan, J., Wang, W., Duggal, N. K., Marr, L. C., Vikesland, P. J., & Zhou, W. M. (2023) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2023.115946 · Cited by 33 · see citing works
Jo, W. K., Schadenhofer, A., Habierski, A., Kaiser, F. K., Saletti, G., Ganzenmueller, T., Hage, E., Haid, S., Pietschmann, T., Hansen, G., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2026558118 · Cited by 33 · see citing works
Modeling within-host and aerosol dynamics of SARS-CoV-2: The relationship with infectiousness
Heitzman-Breen, N., & Ciupe, S. M. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009997 · Cited by 31 · see citing works
Hepp, C., Shiaelis, N., Robb, N. C., Vaughan, A., Matthews, P. C., Stoesser, N. E., Crook, D. W., & Kapanidis, A. N. (2021) · Scientific Reports · doi:10.1038/s41598-021-98972-z · Cited by 32 · see citing works
Tian, Y., Parsons, L. M., Jankowska, E. A., & Cipollo, J. F. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.767448 · Cited by 29 · see citing works
Basile, K., Rockett, R. J., McPhie, K. A., Fennell, M., Johnson-Mackinnon, J. C., Agius, J. E., Fong, W., Rahman, H., Ko, D., Donavan, L., et al. (2022) · Viruses · doi:10.3390/v14092023 · Cited by 30 · see citing works
Patel, D., Field, C., Septer, K. M., Sim, D., Jones, M. J., Heinly, T., Vanderford, T., McGraw, E., & Sutton, T. (2021) · Journal of Virology · doi:10.1128/jvi.02232-20 · Cited by 26 · see citing works
Zilla, M. L., Wheeler, B. J., Keetch, C., Mitchell, G., McBreen, J., Wells, A. H., Shurin, M. R., Peck‐Palmer, O. M., & Wheeler, S. (2020) · American Journal of Clinical Pathology · doi:10.1093/ajcp/aqaa228 · Cited by 28 · see citing works
Self-citationModeling Within-Host Dynamics of SARS-CoV-2 Infection: A Case Study in Ferrets
Vaidya, N. K., Bloomquist, A., & Perelson, A. S. (2021) · Viruses · doi:10.3390/v13081635 · Cited by 27 · see citing works
Sobolik, J. S., Sajewski, E. T., Jaykus, L., Cooper, D. K., Lopman, B. A., Kraay, A. N. M., Ryan, P. B., Guest, J. L., Girard, A. W., & León, J. S. (2021) · Food Control · doi:10.1016/j.foodcont.2022.108845 · Cited by 28 · see citing works
Guo, C., Tsai, S. J., Ai, Y., Li, M., Pekosz, A. S., Cox, A., Atai, N. A., & Gould, S. J. (2022) · Science Advances · doi:10.1126/sciadv.ade5085 · Cited by 29 · see citing works
Liu, Z., Wu, H., Egland, K. A., Gilliland, T. C., Dunn, M. D., Luke, T. C., Sullivan, E. J., Klimstra, W. B., Bausch, C. L., & Whelan, S. P. J. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1940652 · Cited by 26 · see citing works
Self-citationJaworski, E. A., Langsjoen, R. M., Mitchell, B. M., Judy, B. M., Newman, P. C., Plante, J. A., Plante, K. S., Miller, A. L., Zhou, Y., Swetnam, D. M., et al. (2021) · eLife · doi:10.7554/elife.68479 · Cited by 27 · see citing works
Zhdanov, G. A., Nykhrikova, E. V., Meshcheryakova, N. F., Kristavchuk, O. V., Ахметова, А. И., Andreev, E. V., Рудакова, Е. В., Gambaryan, A. S., Yaminsky, I. V., Aralov, A. V., et al. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.937180 · Cited by 27 · see citing works
SARS-CoV-2 Genomic Variation in Space and Time in Hospitalized Patients in Philadelphia
Everett, J. K., Hokama, P., Roche, A. M., Reddy, S. G., Hwang, Y., Kessler, L. R., Glascock, A. L., Li, Y., Whelan, J. N., Weiss, S. R., et al. (2021) · mBio · doi:10.1128/mbio.03456-20 · Cited by 26 · see citing works
Kukushkin, V. I., Kristavchuk, O. V., Andreev, E. V., Meshcheryakova, N. F., Zaborova, O. V., Gambaryan, A. S., Nechaev, A. N., & Zavyalova, E. G. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1076749 · Cited by 24 · see citing works
Systematic Exploration of SARS-CoV-2 Adaptation to Vero E6, Vero E6/TMPRSS2, and Calu-3 Cells
Aiewsakun, P., Phumiphanjarphak, W., Ludowyke, N., Purwono, P. B., Manopwisedjaroen, S., Srisaowakarn, C., Ekronarongchai, S., Suksatu, A., Yuvaniyama, J., & Thitithanyanont, A. (2023) · Genome Biology and Evolution · doi:10.1093/gbe/evad035 · Cited by 26 · see citing works
Basile, K., Rockett, R. J., McPhie, K. A., Fennell, M., Johnson-Mackinnon, J. C., Agius, J. E., Fong, W., Rahman, H., Ko, D., Donavan, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.12.472252 · Cited by 25 · see citing works
Neutralization of SARS-CoV-2 Variants by rVSV-ΔG-Spike-Elicited Human Sera
Yahalom-Ronen, Y., Noam Erez, A., Fisher, M., Tamir, H., Politi, B., Achdout, H., Melamed, S., Glinert, I., Weiss, S., Cohen-Gihon, I., et al. (2022) · Vaccines · doi:10.3390/vaccines10020291 · Cited by 24 · see citing works
Espeseth, A. S., Yuan, M., Citron, M. P., Reiserova, L., Morrow, G., Wilson, A. J., Horton, M. S., Rukhman, M., Kinek, K. C., Hou, F., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104203 · Cited by 24 · see citing works
Multiplex Lithographic SERS Aptasensor for Detection of Several Respiratory Viruses in One Pot
Kukushkin, V. I., Ambartsumyan, O. A., Subekin, A. Y., Astrakhantseva, A. S., Gushchin, V. А., Nikonova, A. A., Dorofeeva, A., Зверев, В. В., Keshek, A. K., Meshcheryakova, N. F., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098081 · Cited by 24 · see citing works
Versatile, Multivalent Nanobody Cocktails Efficiently Neutralize SARS-CoV-2Preprint
Xiang, Y., Nambulli, S., Xiao, Z., Liu, H., Sang, Z., Duprex, W. P., Schneidman-Duhovny, D., Zhang, C., & Shi, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.24.264333 · Cited by 23 · see citing works
Self-citationZou, W., Xiong, M., Hao, S., Zhang, E. Y., Baumlin, N., Kim, M. D., Salathe, M. A., Yan, Z., & Qiu, J. (2021) · mBio · doi:10.1128/mbio.01006-21 · Cited by 22 · see citing works
Isolation of ACE2-dependent and -independent sarbecoviruses from Chinese horseshoe bats
Guo, H., Li, A., Dong, T.-Y., Si, H.-R., Hu, B., Li, B., Zhu, Y., Shi, Z., & Letko, M. C. (2023) · Journal of Virology · doi:10.1128/jvi.00395-23 · Cited by 21 · see citing works
Storti, B., Quaranta, P., Primio, C. D., Clementi, N., Mancini, N., Criscuolo, E., Spezia, P. G., Carnicelli, V., Lottini, G., Paolini, E., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.10.038 · Cited by 20 · see citing works
Zapata-Cardona, M. I., Flórez‐Álvarez, L., Gómez-Gallego, D. M., Moncada-Díaz, M. J., Hernández, J. C., Díaz, F. J., Rugeles, M. T., Aguilar-Jiménez, W., & Zapata, W. (2022) · Iranian Journal of Microbiology · doi:10.18502/ijm.v14i3.9758 · Cited by 21 · see citing works
Frolova, E. I., Palchevska, O., Lukash, T., Domínguez, F. D. B. P., Britt, W. J., & Frolov, I. V. (2022) · Journal of Virology · doi:10.1128/jvi.00753-22 · Cited by 18 · see citing works
Toelzer, C., Gupta, K., Berger, I., & Schaffitzel, C. (2023) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798323000049 · Cited by 16 · see citing works
Gilliland, T. H., Liu, Y., Li, R., Dunn, M., Cottle, E. L., Terada, Y., Ryckman, Z., Alcorn, M. D. H., Vasilatos, S. N., Lundy, J. D., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.07.26.453840 · Cited by 18 · see citing works
Self-citationKnow your enemy and know yourself – the case of SARS-CoV-2 host factors
Lee, W. S., Yousefi, M., Yan, B., Yong, C. L., & Ooi, Y. S. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.007 · Cited by 16 · see citing works
Cochin, M., Touret, F., Driouich, J., Moureau, G., Petit, P.-R., Laprie, C., Solas, C., de Lamballerie, X. N., & Nougaırède, A. (2021) · Antiviral Research · doi:10.1016/j.antiviral.2021.105212 · Cited by 16 · see citing works
Goławski, M., Lewandowski, P., Jabłońska, I., & Delijewski, M. (2022) · Viruses · doi:10.3390/v14050991 · Cited by 16 · see citing works
Human models for COVID‐19 research
Woodall, M. N. J., Masonou, T., Case, K., & Smith, C. M. (2021) · The Journal of Physiology · doi:10.1113/jp281499 · Cited by 13 · see citing works
A non-transmissible live attenuated SARS-CoV-2 vaccine
Adler, J. M., Vidal, R. M., Voß, A., Kunder, S., Nascimento, M., Abdelgawad, A., Langner, C., Vladimirova, D., Osterrieder, N., Gruber, A. D., et al. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2023.05.004 · Cited by 15 · see citing works
Zupin, L., Licen, S., Milani, M., Clemente, L., Martello, L., Semeraro, S., Fontana, F., Ruscio, M., Miani, A., Crovella, S., et al. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph182111172 · Cited by 14 · see citing works
Woodall, M. N. J., Ellis, S., Zhang, S., Kembou-Ringert, J. E., Kite, K., Buggiotti, L., Jacobs, A. I., Agyeman, A. A., Masonou, T., Palor, M., et al. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01233-24 · Cited by 13 · see citing works
Profiling COVID-19 Genetic Research: A Data-Driven Study Utilizing Intelligent Bibliometrics
Wu, M., Zhang, Y., Grosser, M., Tipper, S., Venter, D. J., Lin, H., & Jie Lu, B. (2021) · Frontiers in Research Metrics and Analytics · doi:10.3389/frma.2021.683212 · Cited by 14 · see citing works
Immune durability and protection against SARS-CoV-2 re-infection in Syrian hamsters
Field, C. J., Heinly, T. A., Patel, D., Sim, D. G., Luley, E., Gupta, S. L., Vanderford, T. H., Wrammert, J., & Sutton, T. C. (2022) · Emerging Microbes & Infections · doi:10.1080/22221751.2022.2058419 · Cited by 13 · see citing works
SARS-CoV-2 Portrayed against HIV: Contrary Viral Strategies in Similar Disguise
Duerr, R., Crosse, K. M., Valero-Jimenez, A. M., & Dittmann, M. (2021) · Microorganisms · doi:10.3390/microorganisms9071389 · Cited by 12 · see citing works
Bamford, C., Broadbent, L., Aranday-Cortés, E., McCabe, M., McKenna, J. P., Courtney, D., Touzelet, O., Ali, A., Roberts, G. C., López–Campos, G., et al. (2022) · Viruses · doi:10.3390/v14020325 · Cited by 12 · see citing works
Human organoid systems reveal in vitro correlates of fitness for SARS-CoV-2 B.1.1.7Preprint
Lamers, M. M., Breugem, T. I., Mykytyn, A. Z., Wang, Y., Gröen, N., Knoops, K., Schipper, D., van der Vaart, J., Koopman, C. D., Zhang, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.03.441080 · Cited by 11 · see citing works
Lim, H., Kok, B.-H., Lim, C., Majeed, A. A. A., Leow, C., & Leow, C. (2022) · Biomedical Engineering Advances · doi:10.1016/j.bea.2022.100054 · Cited by 10 · see citing works
Gilliland, T. H., Dunn, M., Liu, Y., Alcorn, M. D. H., Terada, Y., Vasilatos, S. N., Lundy, J. D., Li, R., Nambulli, S., Larson, D. P., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107764 · Cited by 10 · see citing works
Self-citationTargeting spike glycans to inhibit SARS-CoV2 viral entry
Guseman, A. J., Rennick, L. J., Nambulli, S., Roy, C. N., Martinez, D. R., Yang, D. T., Bhinderwala, F., Vergara, S. V., Schaefer, A., Baric, R. S., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2301518120 · Cited by 10 · see citing works
Self-citationGlycosaminoglycan binding by arboviruses: a cautionary tale
Alcorn, M. D. H., & Klimstra, W. B. (2022) · Journal of General Virology · doi:10.1099/jgv.0.001726 · Cited by 10 · see citing works
Self-citationShirato, K., Kakizaki, M., Tomita, Y., Kawase, M., & Takeda, M. (2022) · Pathogens · doi:10.3390/pathogens11030302 · Cited by 10 · see citing works
Nanoisland SERS-Substrates for Specific Detection and Quantification of Influenza A Virus
Zhdanov, G. A., Gambaryan, A. S., Ахметова, А. И., Yaminsky, I. V., Kukushkin, V. I., & Zavyalova, E. G. (2023) · Biosensors · doi:10.3390/bios14010020 · Cited by 9 · see citing works
- Authors
- Klimstra, W. B., Tilston-Lunel, N. L., Nambulli, S., Boslett, J., McMillen, C. M., Gilliland, T., Dunn, M. D., Sun, C., Wheeler, S. E., Wells, A., Hartman, A. L., McElroy, A. K., Reed, D. S., Rennick, L. J., & Duprex, W. P.
- Affiliations
- University of Pittsburgh (US)
- Department of Microbiology and Molecular Genetics, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA
- Corresponding author
- Klimstra, William B.
- Duprex, W. Paul
- ORCID
- Venue
- Journal of General Virology
- Publisher
- Microbiology Society
- Published
- 2020-11-01
- Volume
- 101
- Issue
- 11
- Pages
- 1156-1169
- ISSN
- 0022-1317 (ISSN-L)
- 1465-2099
- PMC
- PMC7879561
- OpenAlex
- W3081204841
- Cited by
- 137
- References
- 69
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 6 · 2023: 20 · 2022: 29 · 2021: 61 · 2020: 13
- FWCI
- 4.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of General Virology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- Dr. Patrick Gallagher, Chancellor of the University of Pittsburgh
- Center for Vaccine Research, University of Pittsburgh
- University of Pittsburgh Clinical and Translational Science Institute
- DSF Charitable Foundation
- National Institutes of Health (AI060525)
- 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 › COVID-19 Clinical Research Studies
- Keywords
- SARS-CoV-2, COVID-19 pandemic, furin cleavage site, spike protein, viral growth, neutralizing antibodies, host range, SARS-CoV, angiotensin-converting enzyme 2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review