The DOI matches its Crossref record; 121 of the 121 references it cites were found in a registry or an index.
SARS-CoV-2 variants, spike mutations and immune escape
Open accessAbstract
Although most mutations in the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome are expected to be either deleterious and swiftly purged or relatively neutral, a small proportion will affect functional properties and may alter infectivity, disease severity or interactions with host immunity. The emergence of SARS-CoV-2 in late 2019 was followed by a period of relative evolutionary stasis lasting about 11 months. Since late 2020, however, SARS-CoV-2 evolution has been characterized by the emergence of sets of mutations, in the context of 'variants of concern', that impact virus characteristics, including transmissibility and antigenicity, probably in response to the changing immune profile of the human population. There is emerging evidence of reduced neutralization of some SARS-CoV-2 variants by postvaccination serum; however, a greater understanding of correlates of protection is required to evaluate how this may impact vaccine effectiveness. Nonetheless, manufacturers are preparing platforms for a possible update of vaccine sequences, and it is crucial that surveillance of genetic and antigenic changes in the global virus population is done alongside experiments to elucidate the phenotypic impacts of mutations. In this Review, we summarize the literature on mutations of the SARS-CoV-2 spike protein, the primary antigen, focusing on their impacts on antigenicity and contextualizing them in the protein structure, and discuss them in the context of observed mutation frequencies in global sequence datasets.
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
“D614G is again associated with the increase in transmissibility, infectivity, and viral load, making the Lambda variant even more lethal [55].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [55]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Each pathogen poses a unique set of challenges, including high lethality, rapid mutations, immune evasion, new strains and variants252–258.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [252]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Mutations in the spike protein and RBD have been shown to affect antibody neutralisation and thus reduce vaccine-induced immunity [22].”
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The Lambda variant spike protein is found to be 3.3 times more resistant to neutralization by the convalescent sera than the parent D614G spike protein and 4.9 times to that of the Alpha variant ones.”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [55]
Experimental — accuracy not yet measuredIn the citing paper
“However, reduced sensitivity of SARS-CoV-2 variants to antibody and serum neutralization has been widely observed (18–21).”
From Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization (2022) · cites this paper as [19]
In the citing paper
“both being immunodominant targets of neutralizing antibodies elicited by COVID-19 vaccines or by SARS-CoV-2 infection (5, 6).”
From Neutralization of SARS-CoV-2 Omicron by BNT162b2 mRNA vaccine–elicited human sera (2022) · cites this paper as [6]
In the citing paper
“However, sequencing data of SARS-CoV-2 from patients revealed persistent accumulation of new mutations over the last two years of the Covid19 pandemic, leading to the emergence of new viral strains that can be more transmissible or virulent5,6 or evade vaccines7–9.”
From The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness (2022) · cites this paper as [8]
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
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
GISAID: Global initiative on sharing all influenza data – from vision to reality
Shu, Y., & McCauley, J. (2017) · Eurosurveillance · doi:10.2807/1560-7917.es.2017.22.13.30494 · Cited by 3,039
A dynamic nomenclature proposal for SARS-CoV-2 lineages to assist genomic epidemiology
Rambaut, A., Holmes, E. C., O’Toole, Á., Hill, V., McCrone, J. T., Ruis, C., du Plessis, L., & Pybus, O. G. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0770-5 · Cited by 2,543
Self-citationTegally, 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
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
Starr, T. N., Greaney, A. J., Hilton, S. K., Ellis, D., Crawford, K. H. D., Dingens, A. S., Navarro, M. J., Bowen, J. E., Tortorici, M. A., Walls, A. C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.012 · Cited by 1,956
Hoffmann, M., Kleine-Weber, H., & Pöhlmann, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.022 · Cited by 1,852
Volz, 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
Self-citationAssessing transmissibility of SARS-CoV-2 lineage B.1.1.7 in England
The COVID-19 Genomics UK (COG-UK) consortium, Volz, E., Mishra, S., Chand, M., Barrett, J. C., Johnson, R., Geidelberg, L., Hinsley, W. R., Laydon, D. J., Dabrera, G., et al. (2021) · Nature · doi:10.1038/s41586-021-03470-x · Cited by 1,611
Self-citationSARS-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
Site-specific glycan analysis of the SARS-CoV-2 spike
Watanabe, Y., Allen, J. D., Wrapp, D., McLellan, J. S., & Crispin, M. (2020) · Science · doi:10.1126/science.abb9983 · Cited by 1,538
Genomics 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
Self-citationThe 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
Piccoli, 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
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
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
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349
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
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
Efficacy of the ChAdOx1 nCoV-19 Covid-19 Vaccine against the B.1.351 Variant
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) · New England Journal of Medicine · doi:10.1056/nejmoa2102214 · Cited by 1,257
Baum, 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
Persistence and Evolution of SARS-CoV-2 in an Immunocompromised Host
Choi, B., Choudhary, M. C., Regan, J., Sparks, J. A., Padera, R. F., Qiu, X., Solomon, I. H., Kuo, H.-H., Boucau, J., Bowman, K., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmc2031364 · Cited by 1,246
Greaney, 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
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
SARS-CoV-2 evolution during treatment of chronic infection
Kemp, S. A., Collier, D. A., Datir, R. P., Ferreira, I. A. T. M., Gayed, S., Jahun, A., Hosmillo, M., Rees-Spear, C., Mlcochova, P., Lumb, I. U., et al. (2021) · Nature · doi:10.1038/s41586-021-03291-y · Cited by 1,097
Self-citationViral targets for vaccines against COVID-19
Dai, L., & Gao, G. F. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00480-0 · Cited by 1,056
Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
Yurkovetskiy, L., Wang, X., Pascal, K. E., Tomkins-Tinch, C., Nyalile, T. P., Wang, Y., Baum, A., Diehl, W. E., Dauphin, A., Carbone, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.032 · Cited by 1,025
Greaney, 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
Evaluating the Effects of SARS-CoV-2 Spike Mutation D614G on Transmissibility and Pathogenicity
Volz, E., Hill, V., McCrone, J. T., Price, A., Jorgensen, D., O’Toole, Á., Southgate, J., Johnson, R., Jackson, B., Nascimento, F. F., et al. (2021) · Cell · doi:10.1016/j.cell.2020.11.020 · Cited by 1,006
Self-citationBeyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein
Casalino, L., Gaieb, Z., Goldsmith, J. A., Hjorth, C. K., Dommer, A. C., Harbison, A. M., Fogarty, C. A., de Barros, E. P., Taylor, B. C., McLellan, J. S., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c01056 · Cited by 925
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
McCallum, M., De Marco, A., Lempp, F. A., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.028 · Cited by 901
N-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 10×
“The substitution L18F has occurred ~21 times in the global population 53 and is associated with escape from multiple NTD-binding mAbs 30 .”
InfluentialSARS-CoV-2 D614G variant exhibits efficient replication ex vivo and transmission in vivo
Hou, Y. J., Chiba, S., Halfmann, P., Ehre, C., Kuroda, M., Dinnon, K. H., Leist, S. R., Schäfer, A., Nakajima, N., Takahashi, K., et al. (2020) · Science · doi:10.1126/science.abe8499 · Cited by 900
Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
Benton, D. J., Wrobel, A. G., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature · doi:10.1038/s41586-020-2772-0 · Cited by 781
Prospective mapping of viral mutations that escape antibodies used to treat COVID-19
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M. C., Dingens, A. S., Li, J. Z., & Bloom, J. D. (2021) · Science · doi:10.1126/science.abf9302 · Cited by 743
Cherian, S., Potdar, V., Jadhav, S., Yadav, P., Gupta, N., Das, M., Rakshit, P., Singh, S., Abraham, P., Panda, S., et al. (2021) · doi:10.1101/2021.04.22.440932 · Cited by 730
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
Self-citationSensitivity 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
Self-citationCherian, S., Potdar, V. A., Jadhav, S., Yadav, P. D., Gupta, N., Das, M., Rakshit, P., Singh, S. K., Abraham, P., Panda, S., et al. (2021) · Microorganisms · doi:10.3390/microorganisms9071542 · Cited by 726
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
Avanzato, V. A., Matson, M. J., Seifert, S. N., Pryce, R., Williamson, B. N., Anzick, S. L., Barbian, K., Judson, S. D., Fischer, E. R., Martens, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.049 · Cited by 720
Viral epitope profiling of COVID-19 patients reveals cross-reactivity and correlates of severity
Shrock, E., Fujimura, E., Kula, T., Timms, R. T., Lee, I.-H., Leng, Y., Robinson, M. L., Sie, B. M., Li, M. Z., Chen, Y., et al. (2020) · Science · doi:10.1126/science.abd4250 · Cited by 678
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Network for Genomic Surveillance in South Africa, Cele, S., COMMIT-KZN Team, Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., et al. (2021) · Nature · doi:10.1038/s41586-021-03471-w · Cited by 651
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
Thomson, E. C., Rosen, L. E., Shepherd, J. G., Spreafico, R., da Silva Filipe, A., Wojcechowskyj, J. A., Davis, C., Piccoli, L., Pascall, D. J., Dillen, J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.037 · Cited by 606
Self-citationEmary, K. R. W., Golubchik, T., Aley, P. K., Ariani, C. V., Angus, B., Bibi, S., Blane, B., Bonsall, D., Cicconi, P., Charlton, S., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00628-0 · Cited by 603
Self-citationWrobel, A. G., Benton, D. J., Xu, P., Roustan, C., Martin, S. R., Rosenthal, P. B., Skehel, J. J., & Gamblin, S. J. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0468-7 · Cited by 544
Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape
McCarthy, K. R., Rennick, L. J., Nambulli, S., Robinson-McCarthy, L. R., Bain, W. G., Haidar, G., & Duprex, W. P. (2021) · Science · doi:10.1126/science.abf6950 · Cited by 535
Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift
Hensley, S. E., Das, S. R., Bailey, A. L., Schmidt, L. M., Hickman, H. D., Jayaraman, A., Viswanathan, K., Raman, R., Sasisekharan, R., Bennink, J. R., et al. (2009) · Science · doi:10.1126/science.1178258 · Cited by 484
Zahradník, J., Marciano, S., Shemesh, M., Zoler, E., Chiaravalli, J., Meyer, B., Rudich, Y., Dym, O., Elad, N., & Schreiber, G. (2021) · doi:10.1101/2021.01.06.425392 · Cited by 458
SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
Zahradník, J., Marciano, S., Shemesh, M., Zoler, E., Harari, D., Chiaravalli, J., Meyer, B., Rudich, Y., Li, C., Marton, I., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00954-4 · Cited by 454
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
SARS-CoV-2 escape 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. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2103154118 · Cited by 429
Spread of a SARS-CoV-2 variant through Europe in the summer of 2020
Hodcroft, E. B., Zuber, M., Nadeau, S., Vaughan, T. G., Crawford, K. H. D., Althaus, C. L., Reichmuth, M. L., Bowen, J. E., Walls, A. C., Corti, D., et al. (2021) · Nature · doi:10.1038/s41586-021-03677-y · Cited by 425
Wu, K., Werner, A. P., Moliva, J. I., Koch, M., Choi, A., Stewart-Jones, G. B. E., Bennett, H., Boyoglu-Barnum, S., Shi, W., Graham, B. S., et al. (2021) · doi:10.1101/2021.01.25.427948 · Cited by 419
Meredith, L. W., Hamilton, W. L., Warne, B., Houldcroft, C. J., Hosmillo, M. D. T., Jahun, A. S., Curran, M. D., Parmar, S., Caller, L., Caddy, S., et al. (2020) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(20)30562-4 · Cited by 387
Self-citationTemporal signal and the phylodynamic threshold of SARS-CoV-2
Duchêne, S., Featherstone, L. A., Haritopoulou-Sinanidou, M., Rambaut, A., Lemey, P., & Baele, G. (2020) · Virus Evolution · doi:10.1093/ve/veaa061 · Cited by 385
Self-citationVulnerabilities in coronavirus glycan shields despite extensive glycosylation
Watanabe, Y., Berndsen, Z. T., Raghwani, J., Seabright, G. E., Allen, J. D., Pybus, O. G., McLellan, J. S., Wilson, I. A., Bowden, T. A., Ward, A. B., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16567-0 · Cited by 377 · cited 2×
“N linked glycans are typically prominent in glycan shielding of virus surface glycoprotein epitopes 33 , although o linked glycans can also contribute 103 .”
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
Genomic characterization of a novel SARS-CoV-2 lineage from Rio de Janeiro, Brazil
Voloch, C. M., da Silva Francisco, R., de Almeida, L. G. P., Cardoso, C. C., Brustolini, O. J., Gerber, A. L., Guimarães, A. P. D. C., Mariani, D., da Costa, R. M., Ferreira, O. C., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00119-21 · Cited by 372
The emergence of SARS-CoV-2 in Europe and North America
Worobey, M., Pekar, J. E., Larsen, B. B., Nelson, M. I., Hill, V., Joy, J. B., Rambaut, A., Suchard, M. A., Wertheim, J. O., & Lemey, P. (2020) · Science · doi:10.1126/science.abc8169 · Cited by 356
Self-citationSARS-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 346
Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.029 · Cited by 345
Emergence and spread of a SARS-CoV-2 variant through Europe in the summer of 2020Preprint
Hodcroft, E. B., Zuber, M., Nadeau, S., Vaughan, T. G., Crawford, K. H. D., Althaus, C. L., Reichmuth, M. L., Bowen, J. E., Walls, A. C., Corti, D., et al. (2020) · medRxiv · doi:10.1101/2020.10.25.20219063 · Cited by 326
D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization
Weissman, D., Alameh, M.-G., de Silva, T., Collini, P., Hornsby, H., Brown, R., LaBranche, C. C., Edwards, R. J., Sutherland, L., Santra, S., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2020.11.012 · Cited by 324
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
Self-citationThe emergence and ongoing convergent evolution of the SARS-CoV-2 N501Y lineages
Martin, D. P., Weaver, S., Tegally, H., San, J. E., Shank, S. D., Wilkinson, E., Lucaci, A. G., Giandhari, J., Naidoo, S., Pillay, Y., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.003 · Cited by 282
Self-citationSweredoski, M. J., & Baldi, P. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn199 · Cited by 263
Recurrent emergence and transmission of a SARS-CoV-2 spike deletion H69/V70
Kemp, S. A., Meng, B., Ferriera, I. A., Datir, R., Harvey, W. T., Papa, G., Lytras, S., Collier, D. A., Mohamed, A., Gallo, G., et al. (2020) · doi:10.1101/2020.12.14.422555 · Cited by 252
Self-citationGreaney, A. J., Loes, A. N., Gentles, L. E., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abi9915 · Cited by 244
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.2021.04.006 · Cited by 243
Kidd, M., Richter, A., Best, A., Cumley, N., Mirza, J., Percival, B., Mayhew, M., Megram, O., Ashford, F., White, T., et al. (2021) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiab082 · Cited by 237
Covid-19: Novavax vaccine efficacy is 86% against UK variant and 60% against South African variant
Mahase, E. (2021) · BMJ · doi:10.1136/bmj.n296 · Cited by 235 · cited 2×
“91 .”
InfluentialKumar, S., Maurya, V. K., Prasad, A. K., Bhatt, M. L. B., & Saxena, S. K. (2020) · VirusDisease · doi:10.1007/s13337-020-00571-5 · Cited by 228
Emergence and expansion of SARS-CoV-2 B.1.526 after identification in New York
Annavajhala, M. K., Mohri, H., Wang, P., Nair, M. S., Zucker, J. E., Sheng, Z., Gomez‐Simmonds, A., Kelley, A. L., Tagliavia, M., Huang, Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03908-2 · Cited by 227
Multiplex qPCR discriminates variants of concern to enhance global surveillance of SARS-CoV-2
Vogels, C. B. F., Breban, M. I., Ott, I. M., Alpert, T., Petrone, M. E., Watkins, A. E., Kalinich, C. C., Earnest, R., Rothman, J. E., de Jesus, J. G., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001236 · Cited by 225
The 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 221
Self-citationTchesnokova, V. L., Kulasekara, H. D., Larson, L., Bowers, V., Rechkina, E., Kisiela, D., Sledneva, Y., Choudhury, D., Maslova, I., Deng, K., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00921-21 · Cited by 214
Covid-19: The E484K mutation and the risks it poses
Wise, J. (2021) · BMJ · doi:10.1136/bmj.n359 · Cited by 211
Genomic Evidence of SARS-CoV-2 Reinfection Involving E484K Spike Mutation, Brazil
Nonaka, C. K. V., Franco, M. M., Gräf, T., Barcia, C. A. D. L., Mendonça, R. N. D. Á., de Sousa, K. A. F., Neiva, L. M. C., Fosenca, V., Mendes, A. V. A., Aguiar, R. S., et al. (2021) · Emerging infectious diseases · doi:10.3201/eid2705.210191 · Cited by 192
CoV-GLUE: A Web Application for Tracking SARS-CoV-2 Genomic Variation
Singer, J., Gifford, R., Cotten, M., & Robertson, D. (2020) · doi:10.20944/preprints202006.0225.v1 · Cited by 167
Self-citationTchesnokova, V., Kulakesara, H., Larson, L., et al. (2021) · bioRxiv · doi:10.1101/2021.02.22.432189 · Cited by 154
Predictive Modeling of Influenza Shows the Promise of Applied Evolutionary Biology
Morris, D. H., Gostic, K. M., Pompei, S., Bedford, T., Łuksza, M., Neher, R. A., Grenfell, B. T., Lässig, M., & McCauley, J. W. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.09.004 · Cited by 148
Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy
Das, S. R., Hensley, S. E., David, A., Schmidt, L., Gibbs, J. S., Puigbò, P., Ince, W. L., Bennink, J. R., & Yewdell, J. W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108754108 · Cited by 143
Neutralization of N501Y mutant SARS-CoV-2 by BNT162b2 vaccine-elicited sera
Xie, X., Zou, J., Fontes-Garfias, C. R., Xia, H., Swanson, K. A., Cutler, M., Cooper, D., Menachery, V. D., Weaver, S., Dormitzer, P. R., et al. (2021) · doi:10.1101/2021.01.07.425740 · Cited by 143
Covid-19: Where are we on vaccines and variants?
Mahase, E. (2021) · BMJ · doi:10.1136/bmj.n597 · Cited by 122
Hu, J., Peng, P., Wang, K., Fang, L., Luo, F.-Y., Jin, A.-S., Liu, B., Tang, N., & Huang, A. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00648-1 · Cited by 111
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 110
Emergence and spread of a SARS-CoV-2 lineage A variant (A.23.1) with altered spike protein in Uganda
Bugembe, D. L., Phan, M. V. T., Ssewanyana, I., Semanda, P., Nansumba, H., Dhaala, B., Nabadda, S. N., O’Toole, Á., Rambaut, A., Kaleebu, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00933-9 · Cited by 104
Self-citationJette, C. A., Cohen, A. A., Gnanapragasam, P. N. P., Muecksch, F., Lee, Y. E., Huey‐Tubman, K. E., Schmidt, F., Hatziioannou, T., Bieniasz, P. D., Nussenzweig, M. C., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109760 · Cited by 99
No evidence for distinct types in the evolution of SARS-CoV-2
MacLean, O. A., Orton, R. J., Singer, J. B., & Robertson, D. L. (2020) · Virus Evolution · doi:10.1093/ve/veaa034 · Cited by 96
Self-citationNeidleman, J. A., Luo, X., McGregor, M. M., Xie, G., Murray, V., Greene, W. C., Lee, S. A., & Roan, N. R. (2021) · eLife · doi:10.7554/elife.72619 · Cited by 89
Three SARS-CoV-2 reinfection cases by the new Variant of Concern (VOC) P.1/501Y.V3Preprint
Naveca, F. G., da Costa, C. F., do Nascimento, V. A., de Souza, V. C., Corado, A. D. L. G., Nascimento, F., Costa, Á., Duarte, D., Silva, G., Mejía, M., et al. (2021) · Research Square · doi:10.21203/rs.3.rs-318392/v1 · Cited by 83
Zheng, Z., Monteil, V., Maurer‐Stroh, S., Yew, C. W., Leong, C., Mohd-Ismail, N. K., Arularasu, S. C., Chow, V. T. K., Lin, R. T. P., Mirazimi, A., et al. (2020) · Eurosurveillance · doi:10.2807/1560-7917.es.2020.25.28.2000291 · Cited by 82
Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New YorkPreprint
West, A. P., Wertheim, J. O., Wang, J. C., Vasylyeva, T. I., Havens, J. L., Chowdhury, M. A., Gonzalez, E., Fang, C. E., Lonardo, S. S. D., Hughes, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.14.431043 · Cited by 74
Huang, B., Dai, L., Wang, H., Hu, Z., Yang, X., Tan, W., & Gao, G. F. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.01.429069 · Cited by 72
Genomic Evidence of a Sars-Cov-2 Reinfection Case With E484K Spike Mutation in BrazilPreprint
Nonaka, C. K. V., Franco, M. M., Gräf, T., Mendes, A. V. A., Aguiar, R. S., Giovanetti, M., & Souza, B. S. D. F. (2021) · Preprints.org · doi:10.20944/preprints202101.0132.v1 · Cited by 64
Soh, W. T., Liu, Y., Nakayama, E. E., Ono, C., Torii, S., Nakagami, H., Matsuura, Y., Shioda, T., & Arase, H. (2020) · doi:10.1101/2020.11.05.369264 · Cited by 61
Neutral Theory and Rapidly Evolving Viral Pathogens
Frost, S. D. W., Magalis, B. R., & Pond, S. L. K. (2018) · Molecular Biology and Evolution · doi:10.1093/molbev/msy088 · Cited by 60
Neutralization of UK-variant VUI-202012/01 with COVAXIN vaccinated human serumPreprint
Sapkal, G. N., Yadav, P. D., Ella, R., Deshpande, G. R., Sahay, R. R., Gupta, N., Mohan, V., Abraham, P., Panda, S., & Bhargava, B. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.26.426986 · Cited by 55
Jette, C. A., Cohen, A. A., Gnanapragasam, P. N. P., Muecksch, F., Lee, Y., Huey-Tubman, K. E., Schmidt, F., Hatziioannou, T., Bieniasz, P., Nussenzweig, M., et al. (2021) · bioRxiv · doi:10.1101/2021.04.23.441195 · Cited by 54
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
Vulnerabilities in coronavirus glycan shields despite extensive glycosylationPreprint
Watanabe, Y., Berndsen, Z. T., Raghwani, J., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.20.957472 · Cited by 49
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) · PubMed · doi:10.34944/dspace/7022 · Cited by 49
Self-citationTablizo, F. A., Kim, K. M., Lapid, C. M., Castro, M. J. R., Yangzon, M. S. L., Maralit, B. A., Ayes, M. E. C., Cutiongco-de la Paz, E. M., De Guzman, A. R., Yap, J. M. C., et al. (2021) · doi:10.1101/2021.03.03.21252812 · Cited by 46
The impact of Spike mutations on SARS-CoV-2 neutralizationPreprint
Rees-Spear, C., Muir, L., Griffith, S. A., Heaney, J., Aldon, Y., Snitselaar, J. L., Pataillot-Meakin, T., Graham, C., Seow, J., Lee, N., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.15.426849 · Cited by 45
Self-citationBugembe, D., V.T.Phan, M., Ssewanyana, I., et al. (2021) · medRxiv · doi:10.1101/2021.02.08.21251393 · Cited by 45
Greaney, A. J., Starr, T. N., Barnes, C., et al. (2021) · bioRxiv · doi:10.1101/2021.03.17.435863 · Cited by 45
PCR assay to enhance global surveillance for SARS-CoV-2 variants of concernPreprint
Vogels, C. B. F., Breban, M. I., Alpert, T., et al. (2021) · medRxiv · doi:10.1101/2021.01.28.21250486 · Cited by 42
Silver, Z. A., Antonopoulos, A., Haslam, S. M., Dell, A., Dickinson, G. M., Seaman, M. S., & Desrosiers, R. C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.056 · Cited by 37
Zhan, X.-Y., Zhang, Y., Zhou, X., Huang, K., Qian, Y., Leng, Y., Yan, L., Huang, B., & He, Y. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.25.170688 · Cited by 29
de 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
Faulkner, N., Ng, K. W., Wu, M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.01.433314 · Cited by 22
Neidleman, J. A., Luo, X., McGregor, M. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.12.443888 · Cited by 20
Greaney, A. J., Loes, A. N., Gentles, L. E., et al. (2021) · bioRxiv · doi:10.1101/2021.04.14.439844 · Cited by 16
A cocktail of antibodies for COVID-19 therapy
Matthews, D. B. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-00431-9 · Cited by 15
CovidExpress: an interactive portal for intuitive investigation on SARS-CoV-2 related transcriptomesPreprint
Djekidel, M. N., Rosikiewicz, W., Peng, J. C., Kanneganti, T., Hui, Y., Jin, H., Hedges, D. J., Schreiner, P. A., Fan, Y., Wu, G., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.14.444026 · Cited by 9
SARS-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
Emergence and Expansion of the SARS-CoV-2 Variant B.1.526 Identified in New York
Annavajhala, M. K., Mohri, H., Wang, P., Nair, M., Zucker, J. E., Sheng, Z., Gomez-Simmonds, A., Kelley, A. L., Tagliavia, M., Huang, Y., et al. (2021) · doi:10.1101/2021.02.23.21252259
Cited by
Sorted by citations
Oral Nirmatrelvir for High-Risk, Nonhospitalized Adults with Covid-19
Hammond, J., Leister-Tebbe, H., Gardner, A., Abreu, P., Bao, W., Wisemandle, W., Baniecki, M., Hendrick, V. M., Damle, B., Simón-Campos, A., et al. (2022) · New England Journal of Medicine · doi:10.1056/nejmoa2118542 · Cited by 2,323
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies
Cao, Y., Wang, J., Jian, F., Xiao, T., Song, W., Yisimayi, A., Huang, W., Li, Q., Wang, P., An, R., et al. (2022) · Nature · doi:10.1038/s41586-021-04385-3 · Cited by 2,006
mRNA vaccines for infectious diseases: principles, delivery and clinical translation
Chaudhary, N., Weissman, D., & Whitehead, K. A. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00283-5 · Cited by 1,555
Cele, S., Jackson, L., Khoury, D. S., Khan, K., Moyo-Gwete, T., Tegally, H., San, J. E., Cromer, D., Scheepers, C., Amoako, D., et al. (2021) · doi:10.1101/2021.12.08.21267417 · Cited by 1,333
“Owing to the large number of mutations in the spike protein and elsewhere on the virus (https://covdb.stanford.edu/page/ mutation-viewer/#omicron), there is concern that this variant will exhibit substantial escape from vaccine-elicited immunity 4,5 .”
Omicron SARS-CoV-2 variant: a new chapter in the COVID-19 pandemic
Karim, S. S. A., & Karim, Q. A. (2021) · The Lancet · doi:10.1016/s0140-6736(21)02758-6 · Cited by 1,302
Metadata
- Authors
- Harvey, W. T., Carabelli, A. M., Jackson, B., Gupta, R. K., Thomson, E. C., Harrison, E. M., Ludden, C., Reeve, R., Rambaut, A., COVID-19 Genomics UK (COG-UK) Consortium, Peacock, S. J., & Robertson, D. L.
- Affiliations
- MRC University of Glasgow Centre for Virus Research (GB)
- University of Cambridge (GB)
- University of Edinburgh (GB)
- Wellcome Sanger Institute (GB)
- University of Glasgow (GB)
- Corresponding author
- Robertson, David L.
- ORCID
- Venue
- Nature Reviews Microbiology
- Published
- 2021-06-01
- Volume
- 19
- Issue
- 7
- Pages
- 409-424
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- PMC
- PMC8167834
- OpenAlex
- W3165479483
- Cited by
- 3,528
- References
- 103
- Citations by year
- 2026: 220 · 2025: 310 · 2024: 475 · 2023: 801 · 2022: 1283 · 2021: 420
- FWCI
- 87.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion, cc-by-sa)
- Northumbria Research Link (Northumbria University) (acceptedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- Apollo (University of Cambridge) (submittedVersion)
- Apollo
- Funders
- Wellcome Trust (Z/17/Z, 206298/Z/17/Z, 220977/Z/20/Z, 220977/Z/20/Z, 206298/Z/17/Z, 206298)
- UK Research and Innovation (MR/W005611/1/, MC_PC_19027)
- National Institute for Health and Care Research
- Academy of Medical Sciences (AMS-CSF4-Torok)
- University of Glasgow
- Directorate for Biological Sciences
- Medical Research Council (MC_UU_12014, MC UU 12014/12, MC_PC_19026, MR/W005611/1, MR/S00291X/1, COVID-19, MR/R024758/1)
- Biotechnology and Biological Sciences Research Council (BB/R012679/1)
- H2020 European Research Council (725422)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- SARS-CoV-2, spike protein mutations, variants of concern, immune evasion, antigenicity, neutralizing antibodies, vaccine effectiveness, vaccine update, viral evolution, mutation frequency, COVID-19 pandemic
- MeSH terms
- COVID-19, SARS-CoV-2, COVID-19 Vaccines, Amino Acids, Epitopes, Antigenic Variation, Humans, Mutation, Protein Conformation, Immune Evasion, 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 ›
Are you an author, or do you see a problem with this page? Request a review