SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination
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Abstract
The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants threatens efforts to contain the coronavirus disease 2019 (COVID-19) pandemic. The number of COVID-19 cases and deaths in India has risen steeply, and a SARS-CoV-2 variant, B.1.617, is believed to be responsible for many of these cases. The spike protein of B.1.617 harbors two mutations in the receptor binding domain, which interacts with the angiotensin converting enzyme 2 (ACE2) receptor and constitutes the main target of neutralizing antibodies. Therefore, we analyze whether B.1.617 is more adept in entering cells and/or evades antibody responses. B.1.617 enters two of eight cell lines tested with roughly 50% increased efficiency and is equally inhibited by two entry inhibitors. In contrast, B.1.617 is resistant against bamlanivimab, an antibody used for COVID-19 treatment. B.1.617 evades antibodies induced by infection or vaccination, although less so than the B.1.351 variant. Collectively, our study reveals that antibody evasion of B.1.617 may contribute to the rapid spread of this variant.
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Of convalescent plasma samples, about 40% had 3-fold to 10-fold and 15% had >10-fold reduced neutralizing activity against the Kappa variant.
“Of convalescent plasma samples, about 40% had 3-fold to 10-fold and 15% had >10-fold reduced neutralizing activity 100,122,234 .”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [234]
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Cites
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
Self-citationSafety and Efficacy of the BNT162b2 mRNA Covid-19 Vaccine
Polack, F. P., Thomas, S. J., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Perez, J. L., Pérez Marc, G., Moreira, E. D., Zerbini, C., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2034577 · Cited by 14,592 · see citing works
Efficacy and Safety of the mRNA-1273 SARS-CoV-2 Vaccine
Baden, L. R., El Sahly, H. M., Essink, B., Kotloff, K., Frey, S., Novak, R., Diemert, D., Spector, S. A., Rouphael, N., Creech, C. B., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2035389 · Cited by 10,119 · 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
A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury
Kuba, K., Imai, Y., Rao, S., Gao, H., Guo, F., Guan, B., Huan, Y., Yang, P., Zhang, Y., Deng, W., et al. (2005) · Nature Medicine · doi:10.1038/nm1267 · Cited by 3,445 · see citing works
Detection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510 · see citing works
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., et al. (2021) · Nature · doi:10.1038/s41586-021-03398-2 · Cited by 2,312 · see citing works
The WHO Rapid Evidence Appraisal for COVID-19 Therapies (REACT) Working Group, Sterne, J. A. C., Murthy, S., Diaz, J. V., Slutsky, A. S., Villar, J., Angus, D. C., Annane, D., Azevedo, L. C. P., Berwanger, O., et al. (2020) · JAMA · doi:10.1001/jama.2020.17023 · Cited by 2,257 · see citing works
Monteil, V., Kwon, H., Prado, P., Hagelkrüys, A., Wimmer, R. A., Stahl, M., Leopoldi, A., Garreta, E., Hurtado del Pozo, C., Prosper, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.004 · Cited by 2,122 · see citing works
Neuropilin-1 facilitates SARS-CoV-2 cell entry and infectivity
Cantuti-Castelvetri, L., Ojha, R., Pedro, L. D., Djannatian, M., Franz, J., Kuivanen, S., van der Meer, F., Kallio, K., Kaya, T., Anastasina, M., et al. (2020) · Science · doi:10.1126/science.abd2985 · Cited by 1,925 · see citing works
Self-citationGenomics and epidemiology of the P.1 SARS-CoV-2 lineage in Manaus, Brazil
Faria, N. R., Mellan, T. A., Whittaker, C., Claro, I. M., Candido, D. D. S., Mishra, S., Crispim, M. A. E., Sales, F. C. S., Hawryluk, I., McCrone, J. T., et al. (2021) · Science · doi:10.1126/science.abh2644 · Cited by 1,461 · see citing works
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
Li, Q., Wu, J., Nie, J., Zhang, L., Hao, H., Liu, S., Zhao, C., Zhang, Q., Liu, H., Nie, L., et al. (2020) · Cell · doi:10.1016/j.cell.2020.07.012 · Cited by 1,420 · see citing works
Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
Garcia-Beltran, W. F., Lam, E. C., St. Denis, K., Nitido, A. D., Garcia, Z. H., Hauser, B. M., Feldman, J., Pavlovic, M. N., Gregory, D. J., Poznansky, M. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.013 · Cited by 1,353 · see citing works
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Wang, Z., Schmidt, F., Weisblum, Y., Muecksch, F., Barnes, C. O., Finkin, S., Schaefer-Babajew, D., Cipolla, M., Gaebler, C., Lieberman, J. A., et al. (2021) · Nature · doi:10.1038/s41586-021-03324-6 · Cited by 1,343 · see citing works
A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2
Shi, R., Shan, C., Duan, X., Chen, Z., Liu, P., Song, J., Song, T., Bi, X., Han, C., Wu, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2381-y · Cited by 1,286 · see citing works
SARS-CoV-2 Neutralizing Antibody LY-CoV555 in Outpatients with Covid-19
Chen, P., Nirula, A., Heller, B., Gottlieb, R. L., Boscia, J., Morris, J., Huhn, G., Cardona, J., Mocherla, B., Stosor, V., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2029849 · Cited by 1,282 · see citing works
Neuropilin-1 is a host factor for SARS-CoV-2 infection
Daly, J. L., Simonetti, B., Klein, K., Chen, K.-E., Williamson, M. K., Antón-Plágaro, C., Shoemark, D. K., Simón-Gracia, L., Bauer, M., Hollandi, R., et al. (2020) · Science · doi:10.1126/science.abd3072 · Cited by 1,251 · see citing works
Tomazini, B. M., Maia, I. S., Cavalcanti, A. B., Berwanger, O., Rosa, R. G., Veiga, V. C., Avezum, A., Lopes, R. D., Bueno, F. R., Silva, M. V. A. O., et al. (2020) · JAMA · doi:10.1001/jama.2020.17021 · Cited by 1,241 · see citing works
Distinct conformational states of SARS-CoV-2 spike protein
Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221 · see citing works
Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail
Hansen, J., Baum, A., Pascal, K. E., Russo, V., Giordano, S., Wloga, E., Fulton, B. O., Yan, Y., Koon, K., Patel, K., et al. (2020) · Science · doi:10.1126/science.abd0827 · Cited by 1,210 · see citing works
Robust neutralizing antibodies to SARS-CoV-2 infection persist for months
Wajnberg, A., Amanat, F., Firpo, A., Altman, D. R., Bailey, M. J., Mansour, M., McMahon, M., Meade, P., Mendu, D. R., Muellers, K., et al. (2020) · Science · doi:10.1126/science.abd7728 · Cited by 1,195 · see citing works
Peng, Y., Mentzer, A. J., Liu, G., Yao, X., Yin, Z., Dong, D., Dejnirattisai, W., Rostron, T., Supasa, P., Liu, C., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0782-6 · Cited by 1,179 · see citing works
SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2
Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Perrett, H. R., Painter, C. D., Narayanan, A., Majowicz, S. A., Kwong, E. M., McVicar, R. N., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.033 · Cited by 1,162 · see citing works
Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Zhou, D., Dejnirattisai, W., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.037 · Cited by 992 · see citing works
SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies
Hoffmann, M., Arora, P., Groß, R., Seidel, A., Hörnich, B. F., Hahn, A. S., Krüger, N., Graichen, L., Hofmann-Winkler, H., Kempf, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.036 · Cited by 897 · see citing works
Self-citationChen, 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
Gottlieb, R., Nirula, A., Chen, P., Boscia, J., Heller, B. N., Morris, J., Huhn, G. D., Cardona, J., Mocherla, B., Stosor, V., et al. (2021) · JAMA · doi:10.1001/jama.2021.0202 · Cited by 857 · see citing works
SARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies
Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R., Walls, A. C., Kemp S, S. A., Bassi, J., Pinto, D., Fregni, C. S., et al. (2021) · doi:10.1101/2021.01.19.21249840 · Cited by 729 · see citing works
Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies
Collier, D. A., De Marco, A., Ferreira, I. A. T. M., Meng, B., Datir, R. P., Walls, A. C., Kemp, S. A., Bassi, J., Pinto, D., Silacci-Fregni, C., et al. (2021) · Nature · doi:10.1038/s41586-021-03412-7 · Cited by 728 · see citing works
Liu, Z., VanBlargan, L. A., Bloyet, L.-M., Rothlauf, P. W., Chen, R. E., Stumpf, S., Zhao, H., Errico, J. M., Theel, E. S., Liebeskind, M. J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.014 · Cited by 725 · see citing works
Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies
Planas, D., Bruel, T., Grzelak, L., Guivel-Benhassine, F., Staropoli, I., Porrot, F., Planchais, C., Buchrieser, J., Rajah, M. M., Bishop, E., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01318-5 · Cited by 697 · see citing works
Leung, K., Shum, M. H., Leung, G. M., Lam, T. T., & Wu, J. T. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.26.1.2002106 · Cited by 694 · see citing works
Functional SARS-CoV-2-Specific Immune Memory Persists after Mild COVID-19
Rodda, L. B., Netland, J., Shehata, L., Pruner, K. B., Morawski, P. A., Thouvenel, C. D., Takehara, K. K., Eggenberger, J., Hemann, E. A., Waterman, H. R., et al. (2021) · Cell · doi:10.1016/j.cell.2020.11.029 · Cited by 647 · see citing works
Xie, X., Liu, Y., Liu, J., Zhang, X., Zou, J., Fontes-Garfias, C. R., Xia, H., Swanson, K. A., Cutler, M., Cooper, D., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01270-4 · Cited by 628 · see citing works
Antibody evasion by the P.1 strain of SARS-CoV-2
Dejnirattisai, W., Zhou, D., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.055 · Cited by 583 · see citing works
Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses
Schmidt, F., Weisblum, Y., Muecksch, F., Hoffmann, H.-H., Michailidis, E., Lorenzi, J. C. C., Mendoza, P., Rutkowska, M., Bednarski, E., Gaebler, C., et al. (2020) · Journal of Experimental Medicine · doi:10.1084/jem.20201181 · Cited by 572 · see citing works
Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine–elicited human sera
Muik, A., Wallisch, A.-K., Sänger, B., Swanson, K. A., Mühl, J., Chen, W., Cai, H., Maurus, D., Sarkar, R., Türeci, Ö., et al. (2021) · Science · doi:10.1126/science.abg6105 · Cited by 515 · see citing works
Wang, S., Qiu, Z., Hou, Y., Deng, X., Xu, W., Zheng, T., Wu, P., Xie, S., Bian, W., Zhang, C., et al. (2021) · Cell Research · doi:10.1038/s41422-020-00460-y · Cited by 486 · see citing works
Starr, T. N., Greaney, A. J., Dingens, A. S., & Bloom, J. D. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100255 · Cited by 470 · see citing works
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera
Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460 · see citing works
Frampton, D., Rampling, T., Cross, A., Bailey, H., Heaney, J., Byott, M., Scott, R., Sconza, R., Price, J., Margaritis, M., et al. (2021) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(21)00170-5 · Cited by 387 · see citing works
Hoffmann, M., Hofmann-Winkler, H., Smith, J. C., Krüger, N., Arora, P., Sørensen, L. K., Søgaard, O. S., Hasselstrøm, J. B., Winkler, M., Hempel, T., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103255 · Cited by 384 · see citing works
Self-citationShen, X., Tang, H., McDanal, C., Wagh, K., Fischer, W., Theiler, J., Yoon, H., Li, D., Haynes, B. F., Sanders, K. O., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.002 · Cited by 378 · see citing works
SARS-CoV-2 501Y.V2 variants lack higher infectivity but do have immune escape
Li, Q., Nie, J., Wu, J., Zhang, L., Ding, R., Wang, H., Zhang, Y., Li, T., Liu, S., Zhang, M., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.042 · Cited by 341 · see citing works
The variant gambit: COVID-19’s next move
Plante, J. A., Mitchell, B. M., Plante, K. S., Debbink, K., Weaver, S. C., & Menachery, V. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.020 · Cited by 328 · see citing works
Graham, M. S., Sudre, C. H., May, A., Antonelli, M., Murray, B., Varsavsky, T., Kläser, K., Canas, L. S., Molteni, E., Modat, M., et al. (2021) · The Lancet Public Health · doi:10.1016/s2468-2667(21)00055-4 · Cited by 304 · see citing works
Berger Rentsch, M., & Zimmer, G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025858 · Cited by 269 · see citing works
SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2Preprint
Clausen, T. M., Sandoval, D. R., Spliid, C. B., Pihl, J., Painter, C. D., Thacker, B. E., Glass, C. A., Narayanan, A., Majowicz, S. A., Yang, Z., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.14.201616 · Cited by 229 · see citing works
Infection- and vaccine-induced antibody binding and neutralization of the B.1.351 SARS-CoV-2 variant
Edara, V. V., Norwood, C., Floyd, K., Lai, L., Davis-Gardner, M. E., Hudson, W. H., Mantus, G., Nyhoff, L. E., Adelman, M. W., Fineman, R., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.009 · Cited by 224 · see citing works
Luan, B., Wang, H., & Huynh, T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14076 · Cited by 192 · see citing works
Kuzmina, A., Khalaila, Y., Voloshin, O., Keren‐Naus, A., Cohen, L. B., Raviv, Y., Shemer‐Avni, Y., Rosenberg, E., & Taube, R. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.008 · Cited by 172 · see citing works
The new SARS-CoV-2 strain shows a stronger binding affinity to ACE2 due to N501Y mutant
Ali, F., Kasry, A., & Amin, M. (2021) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2021.100086 · Cited by 163 · see citing works
Seroprevalence of SARS-CoV-2 in slums versus non-slums in Mumbai, India
Malani, A., Shah, D., Kang, G., Lobo, G. N., Shastri, J. S., Mohanan, M., Jain, R. K., Agrawal, S. R., Juneja, S., Imad, S., et al. (2020) · The Lancet Global Health · doi:10.1016/s2214-109x(20)30467-8 · Cited by 147 · see citing works
Kleine‐Weber, H., Elzayat, M. T., Wang, L., Graham, B. S., Müller, M. A., Drosten, C., Pöhlmann, S., & Hoffmann, M. (2018) · Journal of Virology · doi:10.1128/jvi.01381-18 · Cited by 143 · see citing works
Self-citationJones, B. E., Brown-Augsburger, P., Corbett, K., Westendorf, K., Davies, J., Cujec, T., Wiethoff, C. M., Blackbourne, J., Heinz, B., Foster, D., et al. (2020) · bioRxiv · doi:10.1101/2020.09.30.318972 · Cited by 140 · see citing works
Comparison of Four SARS-CoV-2 Neutralization Assays
Riepler, L., Rössler, A., Falch, A., Volland, A., Borena, W., von Laer, D., & Kimpel, J. (2020) · Vaccines · doi:10.3390/vaccines9010013 · Cited by 117 · see citing works
Hoffmann, M., Müller, M. A., Drexler, J. F., Glende, J., Erdt, M., Gützkow, T., Losemann, C., Binger, T., Deng, H., Schwegmann‐Weßels, C., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072942 · Cited by 112 · see citing works
Self-citationSARS-CoV-2 mutations acquired in mink reduce antibody-mediated neutralization
Hoffmann, M., Zhang, L., Krüger, N., Graichen, L., Kleine‐Weber, H., Hofmann-Winkler, H., Kempf, A. M., Nessler, S., Riggert, J., Winkler, M. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109017 · Cited by 89 · see citing works
Self-citationPrevalence of SARS-CoV-2 in Karnataka, India
Mohanan, M., Malani, A., Krishnan, K., & Acharya, A. (2021) · JAMA · doi:10.1001/jama.2021.0332 · Cited by 51 · see citing works
Brinkmann, C., Hoffmann, M., Lübke, A., Nehlmeier, I., Krämer-Kühl, A., Winkler, M., & Pöhlmann, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0189073 · Cited by 45 · see citing works
Self-citationPrevalence and Time Trend of SARS-CoV-2 Infection in Puducherry, India, August–October 2020
Kar, S. S., Sarkar, S., Murali, S., Dhodapkar, R., Joseph, N. M., & Aggarwal, R. (2021) · Emerging infectious diseases · doi:10.3201/eid2702.204480 · Cited by 16 · see citing works
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Planas, D., Veyer, D., Baidaliuk, A., Staropoli, I., Guivel-Benhassine, F., Rajah, M. M., Planchais, C., Porrot, F., Robillard, N., Puech, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03777-9 · Cited by 1,992 · see citing works
The biological and clinical significance of emerging SARS-CoV-2 variants
Tao, K., Tzou, P. L., Nouhin, J., Gupta, R. K., de Oliveira, T., Kosakovsky Pond, S. L., Fera, D., & Shafer, R. W. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00408-x · Cited by 1,009 · see citing works
Impact of the delta variant on vaccine efficacy and response strategies
Bian, L., Gao, Q., Gao, F., Wang, Q., He, Q., Wu, X., Mao, Q., Xu, M., & Liang, Z. (2021) · Expert Review of Vaccines · doi:10.1080/14760584.2021.1976153 · Cited by 219 · see citing works
Siemieniuk, R. A., Bartoszko, J. J., Díaz Martinez, J. P., Kum, E., Qasim, A., Zeraatkar, D., Izcovich, A., Mangala, S., Ge, L., Han, M. A., et al. (2021) · BMJ · doi:10.1136/bmj.n2231 · Cited by 79 · see citing works
Tackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78 · see citing works
“…regdanvimab) are sensitive to one ormore of themutations found in RBD residues at positions 417, 452, or 484 that are carried by multiple circulating VOCs, including the recently emerging B.1.617 (Hoffmann et al., 2021; McCallum et al., 2021a; Starr et al., 2021b; Wang et al., 2021b) (Figure 5C).”
InfluentialLim, W.-Y., Tan, G. S. E., Htun, H. L., Phua, H. P., Kyaw, W. M., Guo, H., Cui, L., Mak, T. M., Poh, B. F., Wong, J. C. C., et al. (2022) · Journal of Hospital Infection · doi:10.1016/j.jhin.2021.12.011 · Cited by 26 · see citing works
- Authors
- Hoffmann, M., Hofmann-Winkler, H., Krüger, N., Kempf, A., Nehlmeier, I., Graichen, L., Arora, P., Sidarovich, A., Moldenhauer, A.-S., Winkler, M. S., Schulz, S., Jäck, H.-M., Stankov, M. V., Behrens, G. M. N., & Pöhlmann, S.
- Affiliations
- German Primate Center (DE)
- Universitätsmedizin Göttingen (DE)
- Friedrich-Alexander-Universität Erlangen-Nürnberg (DE)
- Medizinische Hochschule Hannover (DE)
- Corresponding author
- Hoffmann, Markus
- Pöhlmann, Stefan
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2021-07
- Volume
- 36
- Issue
- 3
- Pages
- 109415
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC8238662
- OpenAlex
- W3173241791
- Cited by
- 258
- References
- 62
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 18 · 2023: 22 · 2022: 97 · 2021: 108 · 2020: 1
- FWCI
- 19.38
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (01KI2043, 01KI2074A, PO 716/11-1, PO 716/14-1, RTG1660, TRR130)
- Bundesministerium für Bildung und Forschung (01KI2006D, 01KI20328A, 01KI20396, 01KX2021)
- Niedersächsisches Ministerium für Wissenschaft und Kultur (14-76103-184, MWK HZI COVID-19)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Infectious Diseases › COVID-19 Clinical Research Studies
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, Omicron variant, bamlanivimab, antibody escape, viral entry, neutralizing antibodies, COVID-19 vaccines, B.1.351 variant, ACE2 receptor
- MeSH terms
- Angiotensin-Converting Enzyme 2, COVID-19, SARS-CoV-2, COVID-19 Drug Treatment, Antibodies, Viral, Cell Line, Esters, Guanidines, Humans, Protease Inhibitors, Protein Binding, Vaccination, Antibodies, Neutralizing, Antibodies, Monoclonal, Humanized, Spike Glycoprotein, Coronavirus
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 ›
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