Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Open accessPreprint — published as 10.1038/s41586-021-03471-w · Paper page
Abstract
SARS-CoV-2 variants of concern (VOC) have arisen independently at multiple locations and may reduce efficacy of current vaccines targeted at the spike glycoprotein. We re-cently described the emergence of VOC in South Africa (501Y.V2 or PANGO lineage B.1.351) with mutations in the spike receptor-binding domain (RBD) and N-terminal domain (NTD). Here, using a live virus neutralization assay (LVNA), we compared neutralization of a first wave virus (B.1.1.117) versus the 501Y.V2 variant using plasma collected from adults hospitalized with COVID-19 from two South African infection waves, with the second wave dominated by 501Y.V2 infections. Sequencing demonstrated that infections in first wave plasma donors were with viruses harbouring none of the 501Y.V2-defining RBD or NTD mutations, except for one with E484K. 501Y.V2 virus was effectively neutralized by plasma from second wave infections and first wave virus was effectively neutralized by first wave plasma. In cross-neutralization, 501Y.V2 virus was poorly neutralized by first wave plasma, with an 8.4-fold drop in neutralization relative to first wave virus and a 15.1-fold drop relative to 501Y.V2 neutralization by second wave plasma. In contrast, second wave plasma neutralization of first wave virus was more effective, showing 4.1-fold decline relative to 501Y.V2 virus neutralization and 2.3-fold decline relative to first wave plasma neutralization. While we only tested one plasma elicited by E484K alone, this potently neutralized both variants. The observed effective neutralization of first wave virus by 501Y.V2 infection elicited plasma provides preliminary evidence that vaccines based on VOC sequences could retain activity against other circulating SARS-CoV-2 lineages.
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The E484K mutation has been reported to abolish or substantially reduce neutralization by multiple potent monoclonal antibodies and polyclonal convalescent sera in both wild-type and pseudo-virus neutralization assays.
“The E484K mutation has been reported to abolish or substantially reduce neutralization by multiple potent monoclonal antibodies and polyclonal convalescent sera in both wild-type and pseudo-virus neutralization assays.12,13,17,18,22”
From Efficacy of NVX-CoV2373 Covid-19 Vaccine against the B.1.351 Variant (2021) · cites this paper as [12]
A recent report using infectious B.1.351 virus showed that plasma from six convalescent donors was strongly attenuated against this strain, with IC50 values 6- to 200-fold higher than ancestral virus.
“A recent report using infectious B.1.351virus showed that plasma samples from six convalescent donors were strongly attenuated against this strain, with half-maximal inhibitory concentration (IC 50 ) values 6-to 200-fold higher than ancestral virus 29 .”
From Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies (2021) · cites this paper as [29]
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Cites
MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
Katoh, K. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf436 · Cited by 17,027 · cited 3× · see citing works
“It performs alignment of genotypes in MAFFT [29], 168 phylogenetic tree inference in IQ-Tree20, tree dating and ancestral state construction and annotation 169 (https://github.”
BackgroundMethodInfluentialStructure, 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 · cited 1× · see citing works
“V2 variant after outgrowth revealed no changes in the RBD 58 or NTD but a deletion in the furin cleavage site (Table S3) commonly observed after in vitro culture 59 in Vero E6 cells [19, 20].”
BackgroundGrifoni, 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 · cited 2× · see citing works
“However, these vaccines may elicit a broader antibody response and protective T 127 cell immunity [25].”
BackgroundRNA-Based COVID-19 Vaccine BNT162b2 Selected for a Pivotal Efficacy Study
Walsh, E. E., Frenck, R., Falsey, A. R., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Neuzil, K., Mulligan, M. J., Bailey, R., et al. (2020) · doi:10.1101/2020.08.17.20176651 · Cited by 2,615 · see citing works
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2020) · doi:10.1101/2020.12.21.20248640 · Cited by 2,535 · cited 9× · see citing works
“The combination3 of mutations in the 501Y.V2 variant first detected in South Africa include the N501Y,4 K417N, and E484K mutations in the receptor binding domain (RBD) as well as muta-5 tions in the N-terminal domain (NTD).”
BackgroundInfluentialSelf-citationAntibody 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) · doi:10.1101/2021.01.25.428137 · Cited by 2,328
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
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853 · cited 2× · see citing works
“Plasma 50 samples were from blood drawn approximately 1 month post-symptom onset (Table S1), shown to be 51 close to the antibody response peak [16, 17].”
BackgroundSelf-citationEvolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674 · see citing works
Self-citationVolz, E., Mishra, S., Chand, M., Barrett, J. C., Johnson, R., Geidelberg, L., Hinsley, W. R., Laydon, D. J., Dabrera, G., O’Toole, Á., et al. (2021) · doi:10.1101/2020.12.30.20249034 · Cited by 1,611 · cited 2× · see citing works
“[2] Erik Volz, Swapnil Mishra, Meera Chand, Jeffrey C.”
BackgroundSARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599 · cited 3× · see citing works
“All three amino acid residues in the RBD that carry mutations in 501Y.V2 interact directly with the human angiotensin-converting enzyme 2 (hACE2) receptor and form part of the epitopes for hACE2-blocking NAbs [7].”
BackgroundInfluentialPiccoli, L., Park, Y.-J., Tortorici, M. A., Czudnochowski, N., Walls, A. C., Beltramello, M., Silacci-Fregni, C., Pinto, D., Rosen, L. E., Bowen, J. E., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.037 · Cited by 1,395 · 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
Self-citationRamasamy, M. N., Minassian, A. M., Ewer, K. J., Flaxman, A. L., Folegatti, P. M., Owens, D. R., Voysey, M., Aley, P. K., Angus, B., Babbage, G., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)32466-1 · Cited by 1,324 · see citing works
Escape from neutralizing antibodies by SARS-CoV-2 spike protein variants
Weisblum, Y., Schmidt, F., Zhang, F., DaSilva, J., Poston, D., Lorenzi, J. C., Muecksch, F., Rutkowska, M., Hoffmann, H.-H., Michailidis, E., et al. (2020) · eLife · doi:10.7554/elife.61312 · Cited by 1,308 · cited 1× · see citing works
“In a number of separate in vitro studies using monoclonal antibodies (mAbs), mutations at E484 have emerged as immune escape mutations, often conferring broad cross-resistance to panels of mAbs [8, 9, 10, 11].”
BackgroundSnell, G., Czudnochowski, N., Rosen, L. E., Nix, J., Corti, D., Veesler, D., Park, Y., Walls, A., Tortorici, M. A., Cameroni, E., et al. (2020) · doi:10.2210/pdb7jx3/pdb · Cited by 1,267 · cited 7×
“The combination3 of mutations in the 501Y.V2 variant first detected in South Africa include the N501Y,4 K417N, and E484K mutations in the receptor binding domain (RBD) as well as muta-5 tions in the N-terminal domain (NTD).”
BackgroundInfluentialMadhi, S. A., Baillie, V., Cutland, C. L., Voysey, M., Koen, A. L., Fairlie, L., Padayachee, S. D., Dheda, K., Barnabas, S. L., Bhorat, Q. E., et al. (2021) · doi:10.1101/2021.02.10.21251247 · Cited by 1,257 · see citing works
Self-citationBaum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · cited 2× · see citing works
“In a number of separate in vitro studies using monoclonal 33 antibodies (mAbs), mutations at E484 have emerged as immune escape mutations, often conferring broad 34 cross-resistance to panels of mAbs [8, 9, 10, 11].”
BackgroundGreaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · doi:10.1101/2020.12.31.425021 · Cited by 1,178 · cited 2× · see citing works
“[14] Allison J Greaney, Andrea N Loes, Katharine HD Crawford, Tyler N Starr, Keara D Malone, He406 len Y Chu, and Jesse D Bloom.”
BackgroundMethodGreaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R., Crawford, K. H. D., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.007 · Cited by 1,016 · see citing works
Greaney, A. J., Starr, T. N., Gilchuk, P., Zost, S. J., Binshtein, E., Loes, A. N., Hilton, S. K., Huddleston, J., Eguia, R. T., Crawford, K. H. D., et al. (2020) · bioRxiv · doi:10.1101/2020.09.10.292078 · Cited by 948 · cited 1× · see citing works
“In a number of separate in vitro studies using monoclonal 33 antibodies (mAbs), mutations at E484 have emerged as immune escape mutations, often conferring broad 34 cross-resistance to panels of mAbs [8, 9, 10, 11].”
BackgroundN-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · doi:10.1101/2021.01.14.426475 · Cited by 901 · cited 3× · see citing works
“NAbs targeting this site have been shown to be potent neutralizers of SARS-CoV-2 [5, 6].”
BackgroundEvolution of Antibody Immunity to SARS-CoV-2Preprint
Gaebler, C., Wang, Z., Lorenzi, J. C. C., et al. (2020) · bioRxiv · doi:10.1101/2020.11.03.367391 · Cited by 810 · cited 2× · see citing works
“Fitted IC 50 values (Figure 2D) varied between 4 × 10 − 3 for participant 039-13-0013 to 1 × 10 − 4 for participants 039-13-0033 and 039-02-0015, consistent with the previously observed heterogeneity in neutralization between individuals [16, 17].”
BackgroundSelf-citationCirculating SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
Garcia-Beltran, W., Lam, E. C., Denis, K. J. S., et al. (2021) · medRxiv · doi:10.1101/2021.02.14.21251704 · Cited by 781 · 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
Cerutti, G., Guo, Y.-C., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E., Yu, J., Bahna, F., Bimela, J. S., et al. (2021) · bioRxiv · doi:10.1101/2021.01.10.426120 · Cited by 539 · cited 2× · see citing works
“NAbs targeting this site have been shown to be potent neutralizers of SARS-CoV-2 [5, 6].”
BackgroundCell-to-cell spread of HIV permits ongoing replication despite antiretroviral therapy
Sigal, A., Kim, J. T., Balazs, A. B., Dekel, E., Mayo, A., Milo, R., & Baltimore, D. (2011) · Nature · doi:10.1038/nature10347 · Cited by 538 · cited 1× · see citing works
“70 We normalized the number of foci to the number of foci in the absence of plasma on the same plate 71 to obtain the transmission index (Tx, [21]).”
MethodSelf-citationNeutralizing Activity of BNT162b2-Elicited Serum
Liu, Y., Liu, J., Xia, H., Zhang, X., Fontes-Garfias, C. R., Swanson, K. A., Cai, H., Sarkar, R., Chen, W., Cutler, M., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmc2102017 · Cited by 537 · see citing works
Serum Neutralizing Activity Elicited by mRNA-1273 Vaccine
Wu, K., Werner, A. P., Koch, M., Choi, A., Narayanan, E., Stewart-Jones, G. B. E., Colpitts, T., Bennett, H., Boyoglu-Barnum, S., Shi, W., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmc2102179 · Cited by 409 · see citing works
Genomic characterization of a novel SARS-CoV-2 lineage from Rio de Janeiro, Brazil
Voloch, C. M., Silva F, R. D., de Almeida, L. G. P., Cardoso, C. C., Brustolini, O. J., Gerber, A. L., Guimarães, A. P. D. C., Mariani, D., Costa, R. M. D., Ferreira, O. C., et al. (2020) · doi:10.1101/2020.12.23.20248598 · Cited by 372 · cited 2× · see citing works
“Through genomic surveillance of the severe acute respiratory syndrome-related coronavirus 2 (SARS22 CoV-2), a number of new variants have recently been identified with multiple mutations in the spike 23 glycoprotein [1, 2, 3].”
BackgroundDose-response curve slope sets class-specific limits on inhibitory potential of anti-HIV drugs
Shen, L., Peterson, S., Sedaghat, A. R., McMahon, M. A., Callender, M., Zhang, H., Zhou, Y., Pitt, E., Anderson, K. S., Acosta, E. P., et al. (2008) · Nature Medicine · doi:10.1038/nm1777 · Cited by 331 · cited 1× · see citing works
“To obtain the IC50, we fitted the data 76 for each participant to a sigmoidal function [22] with IC50 as the only free parameter (Materials and 77 methods).”
MethodGrowth, detection, quantification, and inactivation of SARS-CoV-2
Case, J. B., Bailey, A. L., Kim, A. S., Chen, R. E., & Diamond, M. (2020) · Virology · doi:10.1016/j.virol.2020.05.015 · Cited by 230 · see citing works
Skelly, D. T., Harding, A. C., Gilbert-Jaramillo, J., Knight, M. L., Longet, S., Brown, A., Adele, S., Adland, E., Brown, H., Team, M. L., et al. (2021) · doi:10.21203/rs.3.rs-226857/v1 · Cited by 216 · see citing works
Cleemput, S., Dumon, W., Fonseca, V., Karim, W. A., Giovanetti, M., Alcantara, L. C., Deforche, K., & de Oliveira, T. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa145 · Cited by 164 · see citing works
Self-citationLiu, 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 · cited 1× · see citing works
“In a number of separate in vitro studies using monoclonal 33 antibodies (mAbs), mutations at E484 have emerged as immune escape mutations, often conferring broad 34 cross-resistance to panels of mAbs [8, 9, 10, 11].”
BackgroundKlimstra, 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., et al. (2020) · Journal of General Virology · doi:10.1099/jgv.0.001481 · Cited by 137 · see citing works
Sigal, A., Milo, R., Cohen, A. A., Geva‐Zatorsky, N., Klein, Y., Alaluf, I., Swerdlin, N., Perzov, N., Danon, T., Liron, Y., et al. (2006) · Nature Methods · doi:10.1038/nmeth892 · Cited by 135 · see citing works
Self-citationLiu, 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. (2020) · doi:10.1101/2020.11.06.372037 · Cited by 135 · cited 1× · see citing works
“E484K also emerged during passage with convalescent 35 plasma, leading to substantial drops in neutralization with convalescent plasma samples [12, 13].”
BackgroundPillay, S., Giandhari, J., Tegally, H., Wilkinson, E., Chimukangara, B., Lessells, R. J., Moosa, M. S., Mattison, S. A., Gazy, I., Fish, M., et al. (2020) · Genes · doi:10.3390/genes11080949 · Cited by 101 · cited 2× · see citing works
“We have previously published full details 158 of the amplification and sequencing protocol [27].”
BackgroundMethodSelf-citationSensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodiesPreprint
Planas, D., Bruel, T., Grzelak, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.12.430472 · Cited by 100 · see citing works
Klimstra, W., Tilston-Lunel, N. L., Nambulli, S., et al. (2020) · bioRxiv · doi:10.1101/2020.06.19.154930 · Cited by 51 · cited 2× · see citing works
“Re-sequencing of the first 501Y.V2 variant after outgrowth revealed no changes in the RBD or NTD but a deletion in the furin cleavage site (Table S3) commonly observed after in vitro culture in Vero E6 cells [19, 20].”
BackgroundPillay, S., Giandhari, J., Tegally, H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.10.144212 · Cited by 30 · see citing works
Self-citationKarim, F., Gazy, I., Cele, S., et al. (2020) · medRxiv · doi:10.1101/2020.11.23.20236828 · Cited by 30 · cited 13× · see citing works
“22Discipline of Virology, University of283 KwaZulu-Natal, School of Laboratory Medicine and Medical Sciences and National Health Laboratory284 Service, Durban, South Africa.”
BackgroundMethodInfluentialSelf-citationMoyano, A., Lustig, G., Rodel, H. E., Tibor Antal, A., & Sigal, A. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007482 · Cited by 8 · cited 1× · see citing works
“Further128 more, it is unclear what degree of neutralization mediates protection, and infection may be particularly 129 sensitive to inhibition at exposure [26].”
BackgroundSelf-citationSARS-CoV-2 escape <i>in vitro</i> from a highly neutralizing COVID-19 convalescent plasma
Andreano, E., Piccini, G., Licastro, D., Casalino, L., Johnson, N. V., Paciello, I., Monego, S. D., Pantano, E., Manganaro, N., Manenti, A., et al. (2020) · doi:10.1101/2020.12.28.424451 · cited 1×
“E484K also emerged during passage with convalescent 35 plasma, leading to substantial drops in neutralization with convalescent plasma samples [12, 13].”
BackgroundSARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
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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
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
Self-citationMultiple 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
“351 lineage, which were recently reported to exhibit nearly complete neutralization resistance in response to convalescent plasma (Cele et al., 2021).”
Self-citationGreaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · see citing works
“Notably, very recent studies on viruses from these lineages largely confirm these predictions from our mapping (Cele et al., 2021; Rees-Spear et al., 2021; Wibmer et al., 2021).”
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · see citing works
Self-citationSensitivity 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
Circulating SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
Garcia-Beltran, W., Lam, E. C., Denis, K. J. S., et al. (2021) · medRxiv · doi:10.1101/2021.02.14.21251704 · Cited by 781 · see citing works
“351 lineage, which were recently reported to exhibit nearly complete neutralization resistance in response to convalescent plasma (Cele et al. 2021).”
Self-citationPreliminary Efficacy of the NVX-CoV2373 Covid-19 Vaccine Against the B.1.351 Variant
Shinde, V., Bhikha, S., Hoosain, Z., Archary, M., Bhorat, Q., Fairlie, L., Lalloo, U., Masilela, M. S. L., Moodley, D., Hanley, S., et al. (2021) · doi:10.1101/2021.02.25.21252477 · Cited by 625 · see citing works
“reported to abolish or substantially reduce neutralization by multiple potent monoclonal antibodies and polyclonal convalescent sera in both wild-type and pseudo-virus neutralization assays.(11,12,16,17,21) Additionally, post-vaccination sera derived from volunteers receiving either of”
BackgroundInfluentialSelf-citationEfficacy of NVX-CoV2373 Covid-19 Vaccine against the B.1.351 Variant
Shinde, V., Bhikha, S., Hoosain, Z., Archary, M., Bhorat, Q., Fairlie, L., Lalloo, U., Masilela, M. S. L., Moodley, D., Hanley, S., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2103055 · Cited by 625 · 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
Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies
Greaney, A. J., Starr, T. N., Barnes, C. O., Weisblum, Y., Schmidt, F., Caskey, M., Gaebler, C., Cho, A., Agudelo, M., Finkin, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24435-8 · Cited by 433 · see citing works
SARS-CoV-2 within-host diversity and transmission
Lythgoe, K., Hall, M. D., Luca Ferretti, A., de Cesare, M., MacIntyre-Cockett, G., Trebes, A., Andersson, M. I., Otecko, N. O., Wise, E. L., Moore, N. A., et al. (2021) · Science · doi:10.1126/science.abg0821 · Cited by 382 · 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
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
SARS-CoV-2 mRNA vaccination induces functionally diverse antibodies to NTD, RBD, and S2
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.005 · Cited by 273 · see citing works
“351 variant RBDs was minor (often only 2-fold) compared to reported reduction in neutralization (which ranges from 6- to 8-fold to complete loss of neutralization) (Cele et al., 2021; Wibmer et al., 2021; Wu et al., 2021).”
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
Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses
Saunders, K. O., Lee, E., Parks, R., Martinez, D. R., Li, D., Chen, H., Edwards, R. J., Gobeil, S., Barr, M., Mansouri, K., et al. (2021) · Nature · doi:10.1038/s41586-021-03594-0 · Cited by 253 · see citing works
Emerging SARS-CoV-2 Variants and Impact in Global Vaccination Programs against SARS-CoV-2/COVID-19
Gómez, C. E., Perdiguero, B., & Estéban, M. (2021) · Vaccines · doi:10.3390/vaccines9030243 · Cited by 262 · see citing works
Genomics and epidemiology of a novel SARS-CoV-2 lineage in Manaus, BrazilPreprint
Faria, N., Mellan, T., Whittaker, C., et al. (2021) · medRxiv · doi:10.1101/2021.02.26.21252554 · Cited by 207 · see citing works
A year of genomic surveillance reveals how the SARS-CoV-2 pandemic unfolded in Africa
Wilkinson, E., Giovanetti, M., Tegally, H., San, J. E., Lessells, R. J., Cuadros, D. F., Martin, D. P., Rasmussen, D. A., Zekri, A. N., Sangaré, A. K., et al. (2021) · Science · doi:10.1126/science.abj4336 · Cited by 213 · see citing works
Self-citationmRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
(2021) · doi:10.1101/2021.01.15.426911 · Cited by 1,354 · see citing works
Self-citationThe effect of spike mutations on SARS-CoV-2 neutralization
Rees-Spear, C., Muir, L., Griffith, S. A., Heaney, J., Aldon, Y., Snitselaar, J. L., Thomas, P., Graham, C., Seow, J., Lee, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108890 · Cited by 215 · see citing works
“351 have been shown to be resistant to neutralization by a large proportion of convalescent plasma samples (Cele et al., 2021; Wibmer et al., 2021).”
Effects of SARS-CoV-2 variants on vaccine efficacy and response strategies
Bian, L., Gao, F., Zhang, J., He, Q., Mao, Q., Xu, M., & Liang, Z. (2021) · Expert Review of Vaccines · doi:10.1080/14760584.2021.1903879 · Cited by 181 · see citing works
“epitopes for hACE2-blocking neutralizing antibodies [18], which might lead to the ineffectiveness of immune protection provided by previous infections and vaccines [19].”
BackgroundEmerging SARS-CoV-2 Variants: A Review of Its Mutations, Its Implications and Vaccine Efficacy
Ramesh, S., Govindarajulu, M., Parise, R. S., Neel, L. T., Shankar, T., Patel, S., Lowery, P., Smith, F., Dhanasekaran, M., & Moore, T. (2021) · Vaccines · doi:10.3390/vaccines9101195 · Cited by 152 · see citing works
SARS-CoV-2 evolution and vaccines: cause for concern?
Williams, T., & Burgers, W. A. (2021) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(21)00075-8 · Cited by 163 · see citing works
Rates of SARS-CoV-2 transmission and vaccination impact the fate of vaccine-resistant strains
Rella, S. A., Kulikova, Y. A., Dermitzakis, E. T., & Kondrashov, F. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-95025-3 · Cited by 136 · see citing works
Jassat, W., Mudara, C., Ozougwu, L., Tempia, S., Blumberg, L. H., Davies, M., Pillay, Y. G., Carter, T., Morewane, R., Wolmarans, M., et al. (2021) · The Lancet Global Health · doi:10.1016/s2214-109x(21)00289-8 · Cited by 190 · see citing works
Hodcroft, E. B., Domman, D., Snyder, D. J., Oguntuyo, K. Y., Diest, M. V., Densmore, K. H., Schwalm, K. C., Femling, J., Carroll, J. L., Scott, R. S., et al. (2021) · medRxiv · doi:10.1101/2021.02.12.21251658 · Cited by 109 · see citing works
SARS-CoV-2 501Y.V2 (B.1.351) elicits cross-reactive neutralizing antibodiesPreprint
Moyo-Gwete, T., Madzivhandila, M., Makhado, Z., Ayres, F., Mhlanga, D., Oosthuysen, B., Lambson, B., Kgagudi, P., Tegally, H., Iranzadeh, A., et al. (2021) · bioRxiv · doi:10.1101/2021.03.06.434193 · Cited by 134 · see citing works
“These confer partial to complete resistance to convalescent plasma and to some monoclonal antibodies (mAbs), including class I/II RBD-directed mAbs and 4A8 which targets the NTD (Wibmer et al., 2021, Cele et al., 2021, Wang et al., 2021a).”
InfluentialSelf-citationCohen, C. A., Li, A. P. Y., Hachim, A., Hui, D. S. C., Kwan, M. Y. W., Tsang, O. T., Chiu, S. S. S., Chan, W. H., Yau, Y. S., Kavian, N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24938-4 · Cited by 138 · see citing works
Madhi, S. A., Baillie, V., Cutland, C. L., Voysey, M., Koen, A. L., Fairlie, L., Padayachee, S. D., Dheda, K., Barnabas, S. L., Bhorat, Q. E., et al. (2021) · doi:10.1101/2021.02.10.21251247 · Cited by 1,257 · see citing works
“351, 25 serum samples from Group-1 participants who tested seronegative at enrolment but showed varying neutralizing antibody titers at 14 days post 2 dose of injection were assayed using PSVNA and LVNA before unblinding of study arm allocation.(14,21) The PSVNA tested neutralization activity against the original D614…”
BackgroundMethodInfluentialSelf-citationGrabowski, F., Preibisch, G., Giziński, S., Kochańczyk, M., & Lipniacki, T. (2021) · Viruses · doi:10.3390/v13030392 · Cited by 112 · see citing works
“shows that an African variant L18F, D80A, D215G, K417N, E484K, N501Y, D614G, A701V propagates much faster than a variant without L18F mutation in the presence of plasma antibodies collected from donors infected in the first wave of epidemic in South Africa (June–August 2020) [28].”
BackgroundCOVID-19 Vaccines: Current Understanding on Immunogenicity, Safety, and Further Considerations
He, Q., Mao, Q., Zhang, J., Bian, L., Gao, F., Wang, J., Xu, M., & Liang, Z. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.669339 · Cited by 108 · see citing works
Hypoxic and Pharmacological Activation of HIF Inhibits SARS-CoV-2 Infection of Lung Epithelial Cells
Wing, P. A. C., Keeley, T. P., Zhuang, X., Lee, Y. S., Prange‐Barczynska, M., Tsukuda, S., Morgan, S. B., Harding, A. C., Argles, I. L. A., Kurlekar, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109020 · Cited by 107 · see citing works
“HV001 (Cele et al., 2021) Centre for the AIDS Programme of Research in South Africa SARS-CoV-2 B1.”
Martin, D. P., Weaver, S., Tegally, H., San, E. J., Shank, S. D., Wilkinson, E., Lucaci, A. G., Giandhari, J., Naidoo, S., Pillay, Y., et al. (2021) · doi:10.1101/2021.02.23.21252268 · Cited by 291 · see citing works
Self-citationChAdOx1 nCoV-19 (AZD1222) protects Syrian hamsters against SARS-CoV-2 B.1.351 and B.1.1.7
Fischer, R. J., van Doremalen, N., Adney, D. R., Yinda, C. K., Port, J. R., Holbrook, M. G., Schulz, J. E., Williamson, B. N., Thomas, T., Barbian, K., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26178-y · Cited by 59 · see citing works
Wyllie, D., Jones, H. E., Mulchandani, R., Trickey, A., Taylor-Phillips, S., Brooks, T., Charlett, A., Ades, A., EDSAB-HOME investigators, Moore, P., et al. (2020) · doi:10.1101/2020.11.02.20222778 · Cited by 96 · 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
An ACE2 Triple Decoy that neutralizes SARS-CoV-2 shows enhanced affinity for virus variants
Tanaka, S., Nelson, G., Olson, C. A., Buzko, O. V., Higashide, W., Shin, A., Gonzalez, M. R., Taft, J. D., Patel, R. S., Buta, S., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-91809-9 · Cited by 64 · see citing works
Redd, A., Nardin, A., Kared, H., et al. (2021) · medRxiv · doi:10.1101/2021.02.11.21251585 · Cited by 65 · see citing works
Cabrera-García, D., Bekdash, R., Abbott, G. W., Yazawa, M., & Harrison, N. L. (2021) · The Journal of Physiology · doi:10.1113/jp281037 · Cited by 71 · see citing works
The ins and outs of SARS-CoV-2 variants of concern (VOCs)
Salehi-Vaziri, ., Fazlalipour, M., Khorrami, S. M. S., Azadmanesh, K., Pouriayevali, M. H., Jalali, T., Shoja, Z., & Maleki, A. (2022) · Archives of Virology · doi:10.1007/s00705-022-05365-2 · Cited by 58 · see citing works
Faulkner, N., Ng, K. W., Wu, M. Y., Harvey, R., Margaritis, M., Paraskevopoulou, S., Houlihan, C., Hussain, S., Greco, M., Bolland, W., et al. (2021) · eLife · doi:10.7554/elife.69317 · Cited by 52 · see citing works
Self-citationRedd, A. D., Nardin, A., Kared, H., Bloch, E. M., Pekosz, A. S., Laeyendecker, O. B., Abel, B., Fehlings, M., Quinn, T. C., & Tobian, A. A. R. (2021) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofab143 · Cited by 105 · see citing works
Skelly, D. T., Harding, A. C., Gilbert-Jaramillo, J., Knight, M. L., Longet, S., Brown, A., Adele, S., Adland, E., Brown, H., Team, M. L., et al. (2021) · doi:10.21203/rs.3.rs-226857/v1 · Cited by 216 · see citing works
Zhuang, X., Tsukuda, S., Wrensch, F., Wing, P. A. C., Schilling, M., Harris, J. M., Borrmann, H., Morgan, S. B., Cane, J., Mailly, L., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103144 · Cited by 62 · see citing works
Amanat, F., Thapa, M., Lei, T., Ahmed, S. M. S., Adelsberg, D. C., Carreño, J. M., Strohmeier, S., Schmitz, A. J., Zafar, S., Zhou, J. Q., et al. (2021) · medRxiv · doi:10.1101/2021.03.07.21253098 · Cited by 41 · see citing works
“Our data indicate that reduction in binding to the E484K and B.1.351 variant RBDs was minor (often only 2-fold) compared to reported reduction in neutralization (which ranges from 6-8 fold to complete loss of neutralization (Cele et al., 2021; Wibmer et al., 2021; Wu et al., 2021)).”
InfluentialPuente, J. H. L., Carreño, J. M., Sun, W., Suárez-Martínez, A., Ramírez-Martínez, L. A., Quezada-Monroy, F., la Rosa, G. P.-D., Vigueras-Moreno, R., Singh, G., Rojas-Martínez, O., et al. (2021) · mBio · doi:10.1128/mbio.01908-21 · Cited by 48 · see citing works
Greaney, A. J., Starr, T. N., Barnes, C., et al. (2021) · bioRxiv · doi:10.1101/2021.03.17.435863 · Cited by 45 · see citing works
SARS‐CoV‐2 virulence evolution: Avirulence theory, immunity and trade‐offs
Alizon, S., & Sofonea, M. T. (2021) · Journal of Evolutionary Biology · doi:10.1111/jeb.13896 · Cited by 46 · see citing works
“Among these mutations, there was the N501Y substitution found in variant α, but also the E484K mutation, which is associated with immune escape (Cele et al., 2021).”
BackgroundLong, S. W., Olsen, R. J., Christensen, P. A., Subedi, S., Olson, R., Davis, J. J., Saavedra, M. O., Yerramilli, P., Pruitt, L., Reppond, K., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.03.004 · Cited by 46 · see citing works
Jassat, W., Mudara, C., Ozougwu, L., Tempia, S., Blumberg, L. H., Davies, M., Pillay, Y. G., Carter, T., Morewane, R., Wolmarans, M., et al. (2021) · medRxiv · doi:10.1101/2021.03.09.21253184 · Cited by 61 · see citing works
“(7,8) The United Kingdom reported increased hospitalisation and mortality rates in people infected with”
BackgroundLusvarghi, S., Wang, W., Herrup, R., Neerukonda, S. N., Vassell, R. A., Bentley, L., Eakin, A. E., Erlandson, K. J., & Weiss, C. D. (2021) · Journal of Virology · doi:10.1128/jvi.01110-21 · Cited by 33 · see citing works
Focosi, D., Tuccori, M., Baj, A., & Maggi, F. (2021) · Viruses · doi:10.3390/v13071211 · Cited by 37 · see citing works
Butera, Y., Mukantwari, E., Artesi, M., Umuringa, J. D., O’Toole, Á., Hill, V., Rooke, S., Hong, S. L., Dellicour, S., Majyambere, O., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25985-7 · Cited by 36 · see citing works
Douglas, J., Geoghegan, J. L., Hadfield, J., Bouckaert, R., Storey, M., Ren, X., de Ligt, J., French, N. P., & Welch, D. (2021) · Emerging infectious diseases · doi:10.3201/eid2709.211097 · Cited by 37 · see citing works
“20248640v) (31), no secondary infections were reported, including in case-patient A’s traveling companion.”
BackgroundThe localized rise of a B.1.526 SARS-CoV-2 variant containing an E484K mutation in New York StatePreprint
Lasek‐Nesselquist, E., Lapierre, P., Schneider, E., George, K. S., & Pata, J. D. (2021) · medRxiv · doi:10.1101/2021.02.26.21251868 · Cited by 38 · see citing works
SARS-COV-2 antibody responses to AZD1222 vaccination in West Africa
Abdullahi, A., Oladele, D. A., Owusu, M., Kemp, S. A., James, A. B., Salako, A. O., Fink, D., Ige, F. A., Ferreira, I. A. T. M., Meng, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33792-x · Cited by 33 · see citing works
Improving family access to dying patients during the COVID-19 pandemic
Downar, J., & Kekewich, M. (2021) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(21)00025-4 · Cited by 35 · see citing works
Hussey, H., Zinyakatira, N., Morden, E., Ismail, M., Paleker, M., Bam, J.-L., London, L., Boulle, A., & Davies, M.-A. (2021) · Gates Open Research · doi:10.12688/gatesopenres.13288.1 · Cited by 27 · see citing works
“However, the science on re-infection is still very unclear, and particularly in the context of emerging variants, this should be interpreted cautiously 23 .”
BackgroundThe Genetic Variant of SARS-CoV-2: Would it matter for Controlling the Devastating Pandemic?
Guo, S., Liu, K., & Zheng, J. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59137 · Cited by 46 · see citing works
Pattabiraman, C., Prasad, P., George, A., et al. (2021) · medRxiv · doi:10.1101/2021.03.17.21253810 · Cited by 24
Ferreira, I. A. T. M., Lee, C. Y. C., Foster, W. S., Abdullahi, A., Dratva, L. M., Tuong, Z. K., Stewart, B. J., Ferdinand, J. R., Guillaume, S. M., Potts, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112991 · Cited by 28 · see citing works
Vaccination with SARS-CoV-2 variants of concern protects mice from challenge with wild-type virus
Amanat, F., Strohmeier, S., Meade, P. S., Dambrauskas, N., Mühlemann, B., Smith, D. J., Vigdorovich, V. I., Sather, D. N., Coughlan, L., & Krammer, F. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001384 · Cited by 19 · see citing works
Hospital mortality in COVID-19 patients in Belgium treated with statins, ACE inhibitors and/or ARBs
Byttebier, G., Belmans, L., Alexander, M., Saxberg, B. E. H., Spiegeleer, B. M. J. D., Spiegeleer, A. D., Devreker, N., Praet, J. T. V., Vanhove, K., Reybrouck, R., et al. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1920271 · Cited by 19 · see citing works
“7) jeopardizes the future effectiveness of antibody treatments (and even vaccines) that target the spike protein of the virus [35-37].”
BackgroundSkelly, D. T., Harding, A. C., Gilbert-Jaramillo, J., Knight, M. L., Longet, S., Brown, A., Adele, S., Adland, E., Brown, H., Team, M. L., et al. (2021) · doi:10.21203/rs.3.rs-226857/v2 · Cited by 216 · see citing works
Self-citationGabitzsch, E., Safrit, J. T., Verma, M., Rice, A., Sieling, P. A., Zakin, L., Shin, A., Morimoto, B., Adisetiyo, H., Wong, R. M. H., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.08.416297 · Cited by 17 · see citing works
“Page 3 INTRODUCTION 47 To address the ongoing COVID-19 pandemic (1, 2), particularly in the face of viral evolution 48 and evidence of viral variant resistance to antibodies and convalescent plasma (3-6), we have 49 developed a vaccine anticipated to protect individuals from SARS-CoV-2 that has the potential to 50 not…”
BackgroundFocosi, D., Franchini, M., Joyner, M. J., & Casadevall, A. (2022) · Vox Sanguinis · doi:10.1111/vox.13239 · Cited by 15 · see citing works
Horspool, A. M., Ye, C., Wong, T. Y., Russ, B. P., Lee, K. S., Winters, M. T., Bevere, J. R., Kieffer, T. W., Martínez, I., Sourimant, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.05.442784 · Cited by 22 · see citing works
“CP exhibited some beneficial effects early in the pandemic for critically ill patients (Bloch, 2020; Bloch et al., 2020; Chen et al., 2020), but its utility has recently been called into question (Casadevall et al., 2021; Cele et al., 2021; NIH, 2021; Zhao and He, 2020).”
BackgroundMethodWurtzer, S., Waldman, P., Levert, M., Mouchel, J., Gorgé, O., Boni, M., Maday, Y., Maréchal, V., & Moulin, L. (2021) · medRxiv · doi:10.1101/2021.03.10.21253291 · Cited by 16 · see citing works
Wagner, R., Meißner, J., Grabski, E., Sun, Y., Vieths, S., & Hildt, E. (2021) · Allergy · doi:10.1111/all.14868 · Cited by 24 · see citing works
Sun, D., Sang, Z., Kim, Y. J., et al. (2021) · bioRxiv · doi:10.1101/2021.03.09.434592 · Cited by 18
“These adaptations led to the global emergence of convergent circulating variants of concern, including the UK strain (B.1.1.7), the South Africa strain (B.1.351), and the Brazil strain (P.1) 22-24 .”
Influentialde Oliveira, T., Lutucuta, S., Nkengasong, J. N., Morais, J. F. M., Paixão, J., Neto, Z., Afonso, P., Miranda, J., David, K., Inglês, L., et al. (2021) · medRxiv · doi:10.1101/2021.03.30.21254323 · Cited by 27 · see citing works
Self-citationOutbreaks of publications about emerging infectious diseases: the case of SARS-CoV-2 and Zika virus
Ipekci, A. M., Buitrago‐García, D., Meili, K. W., Krauer, F., Prajapati, N., Thapa, S., Wildisen, L., Araujo-Chaveron, L., Baumann, L., Shah, S., et al. (2021) · BMC Medical Research Methodology · doi:10.1186/s12874-021-01244-7 · Cited by 16 · see citing works
“For example, preprint publication in December 2020, about the spread of new more infectious variants of SARS-CoV-2 in the United Kingdom and South Africa [30], provided the scientific evidence for strengthening control measures in several European Countries and changing vaccination policy in South Africa.”
BackgroundMolecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
Hendy, M. A., Kaufman, S., & Ponga, M. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-01081-0 · Cited by 17 · see citing works
Deep dissection of the antiviral immune profile of patients with COVID-19
Atanackovic, D., Avila, S. V., Lutfi, F. U., de Miguel‐Pérez, D., Fan, X., Sanchez‐Petitto, G., Mause, E. R. V., Siglin, J., Baddley, J. W., Mannuel, H. D., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02852-1 · Cited by 10 · see citing works
Lyski, Z. L., Brunton, A., Strnad, M. I., et al. (2021) · medRxiv · doi:10.1101/2021.05.28.21258025 · Cited by 12
“Mutations, particularly those in the receptor binding domain (RBD) on the spike protein, have been shown to increase transmissibility through better binding to the host ACE-2 receptor [13-14] as well as reduce antibody-mediated neutralization by human convalescent immune, COVID-19 vaccine sera [9, 15-19] and therapeut…”
BackgroundMultiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity
García-Beltrán, W. F., Lam, E. C., Denis, K. S., Nitido, A. D., Garcia, Z. H., Hauser, B. M., Feldman, J. E., Pavlovic, M., Gregory, D. J., Poznansky, M. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.006 · Cited by 446 · see citing works
“Importantly, these include the spike variants found in two replication-competent live-virus strains of the B.1.351 lineage, which were recently re-ported to exhibit nearly complete neutralization resistance in response to convalescent plasma (Cele et al., 2021).”
InfluentialSelf-citationGenomic Sequencing of SARS-COV-2 in Rwanda: evolution and regional dynamicsPreprint
Butera, Y., Mukantwari, E., Artesi, M., et al. (2021) · medRxiv · doi:10.1101/2021.04.02.21254839 · Cited by 10 · see citing works
Early super-spreader events are a likely determinant of novel SARS-CoV-2 variant predominance
Goyal, A., Reeves, D., & Schiffer, J. (2021) · medRxiv · doi:10.1101/2021.03.23.21254185 · Cited by 10
Novel Highly Divergent SARS-CoV-2 Lineage With the Spike Substitutions L249S and E484K
Laiton‐Donato, K., Usme-Ciro, J. A., Franco-Muñoz, C., Álvarez-Díaz, D. A., Ruiz-Moreno, H. A., Reales-González, J., Prada-Cardozo, D., Corchuelo, S., Herrera-Sepúlveda, M. T., Naizaque, J., et al. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.697605 · Cited by 7 · see citing works
“E484K has been suggested to be responsible for a considerably lower neutralizing activity in vitro from convalescent plasma (20, 24, 25), although the cell-mediated immunity could not be affected by the distinctive mutations (26).”
BackgroundClark, J. J., Sharma, P., Bentley, E. G., Harding, A. C., Kipar, A., Neary, M., Box, H., Hughes, G. L., Patterson, E. I., Sharp, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.10.434447 · Cited by 7 · see citing works
Self-citationMultiplex Fragment Analysis Identifies SARS-CoV-2 Variants
Clark, A. E., Wang, Z.-H., Cantarel, B., et al. (2021) · medRxiv · doi:10.1101/2021.04.15.21253747 · Cited by 7
Lien, C., Kuo, T.-Y., Lin, Y., et al. (2021) · medRxiv · doi:10.1101/2021.03.19.21254000 · Cited by 7
SARS-CoV-2 transmission, vaccination rate and the fate of resistant strains
Rella, S. A., Kulikova, Y. A., Dermitzakis, E., & Kondrashov, F. A. (2021) · medRxiv · doi:10.1101/2021.02.08.21251383 · Cited by 6 · see citing works
Chrysanthus, C. S. (2022) · International Journal of Clinical Virology · doi:10.29328/journal.ijcv.1001043 · Cited by 12 · see citing works
“These aggregated mutations in the 501Y, K417N, and E484K were detected in the receptor-binding domain, RBD including mutations in the N-terminal domain, NTD [11].”
BackgroundWhittaker, C., Watson, O. J., Álvarez, C., Angkasekwinai, N., Boonyasiri, A., Triana, L. C., Chanda, D. M., Charoenpong, L., Chayakulkeeree, M., Cooke, G., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab837 · Cited by 8 · see citing works
Novel Lateral Flow-Based Assay for Simple and Visual Detection of SARS-CoV-2 Mutations
Gomez-Martinez, J., Henry, S., Tuaillon, É., de Perre, P. V., Fournier‐Wirth, C., Foulongne, V., & Brès, J.-C. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.902914 · Cited by 6 · see citing works
“Multiple studies reported that this mutation reduced neutralizing antibody activity, potentially resulting in immune evasion (Cele et al., 2021; Wibmer et al., 2021).”
BackgroundEspinosa, L. A., Ramos, Y., Andújar, I., Torres, E. O., Cabrera, G., Martin, A. M., Gonzalez-Roche, D., Chinea, G., Béquet‐Romero, M., González, I., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.10.443404 · Cited by 4 · see citing works
“SARS-CoV-2 with point mutations (58) or other mutants generated by virus recombination phenomena (59).”
BackgroundImmune dynamics of SARS-CoV-2 virus evolution
Kamat, M., Kurlawala, V., Ghosh, G., & Vaishnav, R. (2022) · International Journal of Molecular and Immuno Oncology · doi:10.25259/ijmio_26_2021 · Cited by 4 · see citing works
Bar‐On, Y. M., Noor, Ε., Gottlieb, N., Sigal, A., & Milo, R. (2021) · medRxiv · doi:10.1101/2021.06.06.21258429 · Cited by 4 · see citing works
Self-citationReview of: "Efficacy of the ChAdOx1 nCoV-19 Covid-19 Vaccine against the B.1.351 Variant"
Lundstrom, K. H. (2021) · Qeios · doi:10.32388/8itiky · Cited by 1 · see citing works
“351 variant was evaluated with pseudovirus and live-virus assays [2,3] in 25 individuals, who were SARS-CoV-2 seronegative at enrolment but showed neutralizing antibody activity against SARS-CoV-2 D614G 14 days after the second vaccination.”
MethodCan proteomics-based approaches further help COVID-19 prevention and therapy?
Kumar, V. (2021) · Expert Review of Proteomics · doi:10.1080/14789450.2021.1924684 · Cited by 6 · see citing works
“351 variants also escape neutralization by convalescent plasma, indicating that the mutant virus can evade the immunity generated by prior SARS-CoV-2 infection [7].”
BackgroundFerreira, I., Lee, C. Q., Foster, W., et al. (2022) · medRxiv · doi:10.1101/2022.10.13.22281024 · Cited by 3
Real-time genomics to track COVID-19 post-elimination border incursions in Aotearoa New Zealand
Douglas, J., Geoghegan, J., Hadfield, J., et al. (2021) · medRxiv · doi:10.1101/2021.05.13.21257194 · Cited by 3
Modelling to inform the COVID-19 response in Bangladesh
Ferguson, E. A., Brum, E., Chowdhury, A., et al. (2021) · medRxiv · doi:10.1101/2021.04.19.21255673 · Cited by 3
- Authors
- Cele, S., Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., Wilkinson, E., Naidoo, Y., Karim, F., Ganga, Y., Khan, K., Bernstein, M., Balazs, A. B., Gosnell, B. I., Hanekom, W., Moosa, M.-Y. S., NGS-SA, COMMIT-KZN Team, Lessells, R. J., Oliveira, T. D., & Sigal, A.
- Affiliations
- Africa Health Research Institute (ZA)
- Hebrew University of Jerusalem (IL)
- Centre for the AIDS Programme of Research in South Africa (ZA)
- University of KwaZulu-Natal (ZA)
- Ragon Institute of MGH, MIT and Harvard (US)
- Max Planck Institute for Infection Biology (DE)
- Corresponding author
- Sigal, Alex
- ORCID
- Cele, Sandile
- Gazy, Inbal
- Jackson, Laurelle
- Hwa, Shi-Hsia
- Tegally, Houriiyah
- Lustig, Gila
- Giandhari, Jennifer
- Pillay, Sureshnee
- Wilkinson, Eduan
- Naidoo, Yeshnee
- Karim, Farina
- Ganga, Yashica
- Khan, Khadija
- Bernstein, Mallory
- Balazs, Alejandro B.
- Gosnell, Bernadett I.
- Hanekom, Willem
- Moosa, Mahomed-Yunus S.
- Lessells, Richard J.
- Oliveira, Tulio de
- Sigal, Alex
- Venue
- Nature
- Publisher
- openRxiv
- Published
- 2021-01-26
- Volume
- 593
- Issue
- 7857
- Pages
- 142-146
- ISSN
- 0028-0836 (ISSN-L)
- PMC
- PMC9867906
- OpenAlex
- W3148277587
- Cited by
- 651
- References
- 29
- Citations by year
- 2026: 13 · 2025: 22 · 2024: 28 · 2023: 63 · 2022: 199 · 2021: 320 · 2020: 3
- FWCI
- 48.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- medRxiv (acceptedVersion, cc-by-nd)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Griffith Research Online (submittedVersion, other-oa)
- Funders
- South African Medical Research Council
- Inyuvesi Yakwazulu-Natali
- National Health Laboratory Service
- Medical Research Council
- National Institute on Drug Abuse (DP2DA040254)
- 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, Beta variant, convalescent plasma, neutralizing antibodies, cross-neutralization, vaccine efficacy, spike protein, receptor binding domain, COVID-19 pandemic, South Africa
- MeSH terms
- COVID-19, SARS-CoV-2, COVID-19 Serotherapy, Animals, Antibodies, Viral, Cell Line, Chlorocebus aethiops, Humans, Immunization, Passive, Mutation, Neutralization Tests, South Africa, Time Factors, Vero Cells, Immune Evasion, Antibodies, Neutralizing
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