The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
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.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredIn the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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×
“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×
“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×
“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
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×
“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
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×
“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
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×
“[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×
“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
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
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
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×
“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
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×
“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×
“[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
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×
“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×
“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×
“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
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
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×
“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×
“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
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
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×
“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 336 · cited 1×
“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 234
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
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
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×
“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].”
BackgroundSigal, A., Milo, R., Cohen, 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 137
Self-citationKlimstra, 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
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. (2020) · doi:10.1101/2020.11.06.372037 · Cited by 135 · cited 1×
“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 103 · cited 2×
“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
Klimstra, W., Tilston-Lunel, N. L., Nambulli, S., et al. (2020) · bioRxiv · doi:10.1101/2020.06.19.154930 · Cited by 51 · cited 2×
“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
Self-citationKarim, F., Gazy, I., Cele, S., et al. (2020) · medRxiv · doi:10.1101/2020.11.23.20236828 · Cited by 30 · cited 13×
“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×
“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 in vitro 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
Cited by
Sorted by citations
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
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
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
“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
“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
Self-citation
Metadata
- 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
- 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
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