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Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines
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Abstract
Understanding the ability of SARS-CoV-2 vaccine-elicited antibodies to neutralize and protect against emerging variants of concern and other sarbecoviruses is key for guiding vaccine development decisions and public health policies. We show that a clinical stage multivalent SARS-CoV-2 receptor-binding domain nanoparticle vaccine (SARS-CoV-2 RBD-NP) protects mice from SARS-CoV-2-induced disease after a single shot, indicating that the vaccine could allow dose-sparing. SARS-CoV-2 RBD-NP elicits high antibody titers in two non-human primate (NHP) models against multiple distinct RBD antigenic sites known to be recognized by neutralizing antibodies. We benchmarked NHP serum neutralizing activity elicited by RBD-NP against a lead prefusion-stabilized SARS-CoV-2 spike immunogen using a panel of single-residue spike mutants detected in clinical isolates as well as the B.1.1.7 and B.1.351 variants of concern. Polyclonal antibodies elicited by both vaccines are resilient to most RBD mutations tested, but the E484K substitution has similar negative consequences for neutralization, and exhibit modest but comparable neutralization breadth against distantly related sarbecoviruses. We demonstrate that mosaic and cocktail sarbecovirus RBD-NPs elicit broad sarbecovirus neutralizing activity, including against the SARS-CoV-2 B.1.351 variant, and protect mice against severe SARS-CoV challenge even in the absence of the SARS-CoV RBD in the vaccine. This study provides proof of principle that sarbecovirus RBD-NPs induce heterotypic protection and enables advancement of broadly protective sarbecovirus vaccines to the clinic.
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“For example, prototypes of multivalent nanoparticle vaccines have been reported to induce broad reactivity against different sarbecoviruses7.”
From Efficacy of an unmodified bivalent mRNA vaccine against SARS-CoV-2 variants in female small animal models (2023) · cites this paper as [7]
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A pneumonia outbreak associated with a new coronavirus of probable bat origin
Zhou, P., Yang, X.-L., Wang, X.-G., Hu, B., Zhang, L., Zhang, W., Si, H.-R., Zhu, Y., Li, B., Huang, C.-L., et al. (2020) · Nature · doi:10.1038/s41586-020-2012-7 · Cited by 21,969
Hoffmann, M., Kleine-Weber, H., Schroeder, S., Krüger, N., Herrler, T., Erichsen, S., Schiergens, T. S., Herrler, G., Wu, N.-H., Nitsche, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.052 · Cited by 20,286 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
Safety and Efficacy of the BNT162b2 mRNA Covid-19 Vaccine
Polack, F. P., Thomas, S. J., Kitchin, N., Absalon, J., Gurtman, A., Lockhart, S., Perez, J. L., Pérez Marc, G., Moreira, E. D., Zerbini, C., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2034577 · Cited by 14,592
Enzymatic assembly of DNA molecules up to several hundred kilobases
Gibson, D. G., Young, L., Chuang, R.-Y., Venter, J. C., Hutchison, C. A., & Smith, H. O. (2009) · Nature Methods · doi:10.1038/nmeth.1318 · Cited by 10,088 · cited 1×
“The RBD-16GS-I53-50A fusion was cloned into pCMV/R using the Xba1 and AvrII restriction sites and Gibson assembly (Gibson et al., 2009).”
Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897 · cited 2×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
BackgroundSelf-citationStructure, 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 5×
“1- with an N-terminal mu-phosphatase signal peptide and a C-terminal octa-histidine tag, flexible linker, and avi tag (GHHHHHHHHGGSSGLNDIFEAQKIEWHE).”
InfluentialSelf-citationStructure 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 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
BackgroundUCSF ChimeraX: Meeting modern challenges in visualization and analysis
Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q. (2020) · Science · doi:10.1126/science.abb2762 · Cited by 5,036 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
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
Structural basis of receptor recognition by SARS-CoV-2
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., & Li, F. (2020) · Nature · doi:10.1038/s41586-020-2179-y · Cited by 3,661 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
An mRNA Vaccine against SARS-CoV-2 — Preliminary Report
Jackson, L. A., Anderson, E. J., Rouphael, N. G., Roberts, P. C., Makhene, M., Coler, R. N., McCullough, M. P., Chappell, J. D., Denison, M. R., Stevens, L. J., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2022483 · Cited by 3,237 · cited 1×
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2
Wang, Q., Zhang, Y., Wu, L., Niu, S., Song, C., Zhang, Z., Lu, G., Qiao, C., Hu, Y., Yuen, K.-Y., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.045 · Cited by 2,892 · cited 1×
“SARS-CoV-2 infects host cells through the attachment of the viral transmembrane spike (S) glycoprotein to angiotensin-converting enzyme 2 (ACE2), followed by fusion of the viral and host membranes (Hoffmann et al., 2020; Lan et al., 2020; Letko et al., 2020; Shang et al., 2020; Walls et al., 2020a; Wang et al., 2020;…”
Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England
Davies, N. G., Abbott, S., Barnard, R. C., Jarvis, C. I., Kucharski, A. J., Munday, J. D., Pearson, C. A. B., Russell, T. W., Tully, D. C., Washburne, A. D., et al. (2021) · Science · doi:10.1126/science.abg3055 · Cited by 2,581
Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England
Davies, N. G., Abbott, S., Barnard, R. C., Jarvis, C. I., Kucharski, A. J., Munday, J. D., Pearson, C. A. B., Russell, T. W., Tully, D. C., Washburne, A. D., et al. (2020) · doi:10.1101/2020.12.24.20248822 · Cited by 2,557 · cited 2×
“2 (delta) that originated in the UK, South Africa, the USA, Brazil, and India, respectively (Davies et al., 2020; Deng et al., 2021; Faria et al., 2021; McCallum et al., 2021b; Tegally et al., 2020).”
InfluentialTegally, 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 1×
“2 (delta) that originated in the UK, South Africa, the USA, Brazil, and India, respectively (Davies et al., 2020; Deng et al., 2021; Faria et al., 2021; McCallum et al., 2021b; Tegally et al., 2020).”
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
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
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
Self-citationCross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885 · cited 20×
“Genes encoding CR3022 heavy and light chains were ordered fromGenScript and cloned into pCMV/R. S309 construct as previously described (Pinto et al., 2020).”
InfluentialSelf-citationIdentifying SARS-CoV-2-related coronaviruses in Malayan pangolins
Lam, T. T., Jia, N., Zhang, Y.-W., Shum, M. H.-H., Jiang, J.-F., Zhu, H., Tong, Y., Shi, Y., Ni, X.-B., Liao, Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2169-0 · Cited by 1,877 · cited 1×
“7 3 10(2) VSV) and RaTG13 (GMT VSV 6 3 10(2)) (Figures 3E and 3F) (Lam et al., 2020; Zhou et al., 2020b), in agreement with the close phylogenetic relationship of their RBDs with that of SARS-CoV-2 S (Figure S2B).”
SARS-CoV-2 mRNA Vaccine Design Enabled by Prototype Pathogen Preparedness
Corbett, K. S., Edwards, D. K., Leist, S. R., Abiona, O. M., Boyoglu-Barnum, S., Gillespie, R. A., Himansu, S., Schäfer, A., Ziwawo, C. T., DiPiazza, A. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2622-0 · Cited by 1,615
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
Spike mutation D614G alters SARS-CoV-2 fitness
Plante, J. A., Liu, Y., Liu, J., Xia, H., Johnson, B. A., Lokugamage, K. G., Zhang, X., Muruato, A. E., Zou, J., Fontes-Garfias, C. R., et al. (2021) · Nature · doi:10.1038/s41586-020-2895-3 · Cited by 1,558
A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV
Yuan, M., Wu, N. C., Zhu, X., Lee, C.-C. D., So, R. T. Y., Lv, H., Mok, C. K. P., & Wilson, I. A. (2020) · Science · doi:10.1126/science.abb7269 · Cited by 1,429 · cited 15×
“Genes encoding CR3022 heavy and light chains were ordered fromGenScript and cloned into pCMV/R. S309 construct as previously described (Pinto et al., 2020).”
InfluentialThe 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 · cited 1×
“Conversely, some mutations found in circulating SARS-CoV-2 isolates were shown to promote escape from mAbs and to reduce neutralization by immune sera (Baum et al., 2020b; Collier et al., 2021; Li et al., 2020; McCallum et al., 2021a, 2021b; Wang et al., 2021a; Weisblum et al., 2020; Wibmer et al., 2021).”
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 · cited 22×
“Genes encoding CR3022 heavy and light chains were ordered fromGenScript and cloned into pCMV/R. S309 construct as previously described (Pinto et al., 2020).”
InfluentialSelf-citationmRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
(2021) · doi:10.1101/2021.01.15.426911 · Cited by 1,354
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 · cited 1×
“Conversely, some mutations found in circulating SARS-CoV-2 isolates were shown to promote escape from mAbs and to reduce neutralization by immune sera (Baum et al., 2020b; Collier et al., 2021; Li et al., 2020; McCallum et al., 2021a, 2021b; Wang et al., 2021a; Weisblum et al., 2020; Wibmer et al., 2021).”
Structure-based design of prefusion-stabilized SARS-CoV-2 spikes
Hsieh, C.-L., Goldsmith, J. A., Schaub, J. M., DiVenere, A. M., Kuo, H.-C., Javanmardi, K., Le, K. C., Wrapp, D., Lee, A. G., Liu, Y., et al. (2020) · Science · doi:10.1126/science.abd0826 · Cited by 1,303
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
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 · cited 4×
“To understand the impact of the full constellation of mutations present in the S proteins of the aforementioned VOCs, we evaluated RBD-NP- andHexaPro S-elicited serum neutralizing activity against corresponding HIV and VSV pseudotyped variants (D614G GMT RBD-NP HIV 5 3 103 and VSV RBD-NP 6 3 102, respectively, and D61…”
InfluentialRogers, T. F., Zhao, F., Huang, D., Beutler, N., Burns, A., He, W.-T., Limbo, O., Smith, C., Song, G., Woehl, J., et al. (2020) · Science · doi:10.1126/science.abc7520 · Cited by 1,230 · cited 1×
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
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
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 · cited 12×
“These findings show that, as is the case for many convalescent individuals (Greaney et al., 2021b; Liu et al., 2021; Piccoli et al., 2020), an important fraction of vaccine-elicited neutralizing Abs in NHPs and humans is focused on the RBM (specifically around position 484), independently of the immunogen (RBD-NP, Hex…”
InfluentialSelf-citationSARS-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 · cited 1×
“Conversely, some mutations found in circulating SARS-CoV-2 isolates were shown to promote escape from mAbs and to reduce neutralization by immune sera (Baum et al., 2020b; Collier et al., 2021; Li et al., 2020; McCallum et al., 2021a, 2021b; Wang et al., 2021a; Weisblum et al., 2020; Wibmer et al., 2021).”
Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability
Brouwer, P. J. M., Caniels, T. G., van der Straten, K., Snitselaar, J. L., Aldon, Y., Bangaru, S., Torres, J. L., Okba, N. M. A., Claireaux, M., Kerster, G., et al. (2020) · Science · doi:10.1126/science.abc5902 · Cited by 1,140 · cited 1×
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
BackgroundImmunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen
Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073 · cited 14×
“(D) SARS-CoV-2 S2P (left) or SARS-CoV S2P (right) Ab binding titers of RBD-NP-elicited sera in pigtail macaques (magenta) or HexaPro S-elicited sera in rhesus macaques (gray) analyzed by ELISA with an LOD of 2.53 101.”
InfluentialSelf-citationCorrelates of Protection Against SARS-CoV-2 in Rhesus Macaques
McMahan, K., Yu, J., Mercado, N. B., Loos, C., Tostanoski, L. H., Chandrashekar, A., Liu, J., Peter, L., Atyeo, C., Zhu, A., et al. (2021) · Nature · doi:10.1038/s41586-020-03041-6 · Cited by 1,068 · cited 1×
“serum neutralizing Ab titers than mice receiving a single 1-mg dose, suggesting that they would likely also be protected since neutralizing Ab titers are a correlate of protection against SARS-CoV-2 (Arunachalam et al., 2021; McMahan et al., 2021).”
Evaluation of the mRNA-1273 Vaccine against SARS-CoV-2 in Nonhuman Primates
Corbett, K. S., Flynn, B., Foulds, K. E., Francica, J. R., Boyoglu-Barnum, S., Werner, A. P., Flach, B., O’Connell, S., Bock, K. W., Minai, M., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2024671 · Cited by 1,066
Self-citationPotently neutralizing and protective human antibodies against SARS-CoV-2
Zost, S. J., Gilchuk, P., Case, J. B., Binshtein, E., Chen, R. E., Nkolola, J. P., Schäfer, A., Reidy, J. X., Trivette, A., Nargi, R. S., et al. (2020) · Nature · doi:10.1038/s41586-020-2548-6 · Cited by 1,041 · cited 1×
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
Self-citationStructural 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 · cited 1×
“The SARS-CoV-2 S D614G mutation has become globally dominant and is associated with enhanced viral transmission and replication but does not significantly affect Abmediated neutralization (Hou et al., 2020; Korber et al., 2020; Plante et al., 2020; Yurkovetskiy et al., 2020).”
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 · cited 16×
“O/W VFI N/A TMB SeraCare Cat# 5120-0083 Thrombin Sigma Cat# T9326-150UN Immobilized Papain ThermoScientific Cat# 20341 LysC-endoproteinase NEB Cat# P8109S EZ-Link Sulfo-NHS-LC Biotinylation Kit Thermo Fisher Scientific Cat#21435 Experimental models: Cell lines Expi 293F ThermoFisher Cat #A14527 HEK-ACE2 adherent BEI (…”
InfluentialSelf-citationDNA vaccine protection against SARS-CoV-2 in rhesus macaques
Yu, J., Tostanoski, L. H., Peter, L., Mercado, N. B., McMahan, K., Mahrokhian, S. H., Nkolola, J. P., Liu, J., Li, Z., Chandrashekar, A., et al. (2020) · Science · doi:10.1126/science.abc6284 · Cited by 997 · cited 1×
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Self-citationA SARS-like cluster of circulating bat coronaviruses shows potential for human emergence
Menachery, V. D., Yount, B. L., Debbink, K. M., Agnihothram, S., Gralinski, L. E., Plante, J. A., Graham, R. L., Scobey, T., Ge, X., Donaldson, E., et al. (2015) · Nature Medicine · doi:10.1038/nm.3985 · Cited by 901
Self-citationN-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
Self-citationSARS-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 · cited 1×
“The SARS-CoV-2 S D614G mutation has become globally dominant and is associated with enhanced viral transmission and replication but does not significantly affect Abmediated neutralization (Hou et al., 2020; Korber et al., 2020; Plante et al., 2020; Yurkovetskiy et al., 2020).”
BackgroundSelf-citationSingle-Shot Ad26 Vaccine Protects Against SARS-CoV-2 in Rhesus Macaques
Mercado, N. B., Zahn, R., Wegmann, F., Loos, C., Chandrashekar, A., Yu, J., Liu, J., Peter, L., McMahan, K., Tostanoski, L. H., et al. (2020) · Nature · doi:10.1038/s41586-020-2607-z · Cited by 789 · cited 1×
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Self-citationStructural Basis for RNA Replication by the SARS-CoV-2 Polymerase
Wang, Q., Wu, J., Wang, H., Gao, Y., Liu, Q., Mu, A., Ji, W., Yan, L., Zhu, Y., Zhu, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.034 · Cited by 773
Structural insights into coronavirus entry
(2019) · Advances in Virus Research · doi:10.1016/bs.aivir.2019.08.002 · Cited by 769 · cited 1×
“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationCrawford, K. H. D., Eguia, R. T., Dingens, A. S., Loes, A. N., Malone, K. D., Wolf, C. R., Chu, H. Y., Tortorici, M. A., Veesler, D., Murphy, M., et al. (2020) · Viruses · doi:10.3390/v12050513 · Cited by 744 · cited 2×
“HIV-based pseudotypes were prepared as previously described (Crawford et al., 2020).”
Self-citationProspective 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
Self-citationSARS-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-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. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.01.014 · Cited by 725 · cited 1×
“These findings show that, as is the case for many convalescent individuals (Greaney et al., 2021b; Liu et al., 2021; Piccoli et al., 2020), an important fraction of vaccine-elicited neutralizing Abs in NHPs and humans is focused on the RBM (specifically around position 484), independently of the immunogen (RBD-NP, Hex…”
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
Traggiai, E., Becker, S., Subbarao, K., Kolesnikova, L., Uematsu, Y., Gismondo, M. R., Murphy, B. R., Rappuoli, R., & Lanzavecchia, A. (2004) · Nature Medicine · doi:10.1038/nm1080 · Cited by 697
Self-citationA mouse-adapted model of SARS-CoV-2 to test COVID-19 countermeasures
Dinnon, K. H., Leist, S. R., Schäfer, A., Edwards, C. E., Martinez, D. R., Montgomery, S. A., West, A., Yount, B. L., Hou, Y. J., Adams, L. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2708-8 · Cited by 675
Self-citationTransmission, 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 · cited 2×
“2 (delta) that originated in the UK, South Africa, the USA, Brazil, and India, respectively (Davies et al., 2020; Deng et al., 2021; Faria et al., 2021; McCallum et al., 2021b; Tegally et al., 2020).”
InfluentialProspective mapping of viral mutations that escape antibodies used to treat COVID-19Preprint
Starr, T. N., Greaney, A. J., Addetia, A., Hannon, W. W., Choudhary, M., Dingens, A. S., Li, J. Z., & Bloom, J. (2020) · bioRxiv · doi:10.1101/2020.11.30.405472 · Cited by 633 · cited 6×
“The 16-nucleotide barcode sequences identifying each RBD variant were amplified by PCR and sequenced on an Illumina HiSeq 2500 with 50 bp single-end reads as described in Greaney et al. (2020 and Starr et al. (2020a).”
InfluentialSelf-citationA Mouse-Adapted SARS-CoV-2 Induces Acute Lung Injury and Mortality in Standard Laboratory Mice
Leist, S. R., Dinnon, K. H., Schäfer, A., Tse, L. V., Okuda, K., Hou, Y. J., West, A., Edwards, C. E., Sanders, W., Fritch, E. J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.050 · Cited by 613 · cited 10×
“These results indicate that one or two immunizations with 1 mg RBD-NPs results in protection against SARS-CoV-2 MA10-induced disease.”
MethodInfluentialSelf-citationThomson, 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-citationter Meulen, J., van den Brink, E. N., Poon, L. L. M., Marissen, W. E., Leung, C. S.-W., Cox, F., Cheung, C. Y., Bakker, A. Q., Bogaards, J. A., van Deventer, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030237 · Cited by 599
Zhou, H., Chen, X., Hu, T., Li, J., Song, H., Liu, Y., Wang, P., Liu, D., Yang, J., Holmes, E. C., et al. (2020) · Current Biology · doi:10.1016/j.cub.2020.05.023 · Cited by 589 · cited 3×
“…viruses harboring the S glycoprotein of the Pangolin-GD isolate (GMT 6.6 3 102 and 7.7 3 102 VSV) and RaTG13 (GMT VSV 6 3 102) (Figures 3E and 3F) (Lam et al., 2020; Zhou et al., 2020b), in agreement with the close phylogenetic relationship of their RBDs with that of SARS-CoV-2 S (Figure S2B).”
InfluentialUnexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion
Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., et al. (2019) · Cell · doi:10.1016/j.cell.2018.12.028 · Cited by 582
Self-citationAccurate design of megadalton-scale two-component icosahedral protein complexes
Bale, J. B., Gonen, S., Liu, Y., Sheffler, W., Ellis, D., Thomas, C. P., Cascio, D., Yeates, T. O., Gonen, T., King, N. P., et al. (2016) · Science · doi:10.1126/science.aaf8818 · Cited by 567 · cited 2×
“We recently described a multivalent subunit vaccine displaying the SARS-CoV-2 RBD nanoparticle (RBD-NP) in a highly immunogenic array using a computationally designed selfassembling protein nanoparticle (Bale et al., 2016; Walls et al., 2020b).”
Self-citationmRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
Stamatatos, L., Czartoski, J., Wan, Y.-H., Homad, L. J., Rubin, V., Glantz, H., Neradilek, M., Seydoux, E., Jennewein, M. F., MacCamy, A. J., et al. (2021) · Science · doi:10.1126/science.abg9175 · Cited by 557
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 · cited 4×
“To understand the impact of the full constellation of mutations present in the S proteins of the aforementioned VOCs, we evaluated RBD-NP- andHexaPro S-elicited serum neutralizing activity against corresponding HIV and VSV pseudotyped variants (D614G GMT RBD-NP HIV 5 3 103 and VSV RBD-NP 6 3 102, respectively, and D61…”
BackgroundInfluentialCryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
Walls, A. C., Tortorici, M. A., Bosch, B., Frenz, B., Rottier, P. J. M., DiMaio, F., Rey, F. A., & Veesler, D. (2016) · Nature · doi:10.1038/nature16988 · Cited by 533
Self-citationWalls, A. C., Fiala, B., Schäfer, A., Wrenn, S., Pham, M. N., Murphy, M., Tse, L. V., Shehata, L., O’Connor, M. A., Chen, C., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.043 · Cited by 532
Self-citationBroad neutralization of SARS-related viruses by human monoclonal antibodies
Wec, A. Z., Wrapp, D., Herbert, A. S., Maurer, D. P., Haslwanter, D., Sakharkar, M., Jangra, R. K., Dieterle, M. E., Lilov, A., Huang, D., et al. (2020) · Science · doi:10.1126/science.abc7424 · Cited by 526 · cited 2×
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
Self-citationREGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters
Baum, A., Ajithdoss, D., Copin, R., Zhou, A., Lanza, K., Negron, N., Ni, M., Wei, Y., Mohammadi, K., Musser, B., et al. (2020) · Science · doi:10.1126/science.abe2402 · Cited by 517
Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
Tortorici, M. A., Beltramello, M., Lempp, F. A., Pinto, D., Dang, H. V., Rosen, L. E., McCallum, M., Bowen, J., Minola, A., Jaconi, S., et al. (2020) · Science · doi:10.1126/science.abe3354 · Cited by 510 · cited 1×
“Numerous monoclonal Abs (mAbs) recognizing distinct antigenic sites on the RBD were isolated and shown to neutralize viral entry and protect small animals and non-human primates (NHPs) from SARS-CoV-2 challenge (Barnes et al., 2020; Baum et al., 2020a; Brouwer et al., 2020; Piccoli et al., 2020; Pinto et al., 2020; Ro…”
Self-citationSARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 503 · cited 13×
“The isolation of RBD-specific cross-reactive mAbs neutralizing SARS-CoV-2 and SARS-CoV suggests that RBD-based vaccines could, in principle, elicit Abs that neutralize distantly related sarbecoviruses, which have future pandemic potential (Cathcart et al., 2021; Jette et al., 2021; Martinez et al., 2021a; Pinto et al.…”
InfluentialSelf-citationBolles, M., Deming, D., Long, K., Agnihothram, S., Whitmore, A., Ferris, M., Funkhouser, W., Gralinski, L., Totura, A., Heise, M., et al. (2011) · Journal of Virology · doi:10.1128/jvi.06048-11 · Cited by 477 · cited 2×
“Previous studies showed that double-inactivated SARS-CoV vaccines could lead to eosinophil infiltration in the lungs and subsequent immune pathology (Bolles et al., 2011).”
BackgroundSelf-citationA Mouse-Adapted SARS-Coronavirus Causes Disease and Mortality in BALB/c Mice
Roberts, A., Deming, D., Paddock, C. D., Cheng, A., Yount, B. L., Vogel, L., Herman, B. D., Sheahan, T., Heise, M. T., Genrich, G. L., et al. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030005 · Cited by 447
Self-citationSARS-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
Self-citationSARS-like WIV1-CoV poised for human emergence
Menachery, V. D., Yount, B. L., Sims, A. C., Debbink, K., Agnihothram, S. S., Gralinski, L. E., Graham, R. L., Scobey, T., Plante, J. A., Royal, S. R., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517719113 · Cited by 418
Self-citationSARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
McCallum, M., Bassi, J., De Marco, A., Chen, A., Walls, A. C., Di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · Science · doi:10.1126/science.abi7994 · Cited by 412
Self-citationSerum 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
Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice
Cohen, A. A., Gnanapragasam, P. N. P., Lee, Y. E., Hoffman, P. R., Ou, S. K.-H., Kakutani, L. M., Keeffe, J. R., Wu, H., Howarth, M. R., West, A. P., et al. (2021) · Science · doi:10.1126/science.abf6840 · Cited by 396
Broad betacoronavirus neutralization by a stem helix–specific human antibody
Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 385 · cited 1×
“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationThe antigenic anatomy of SARS-CoV-2 receptor binding domain
Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371
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 · cited 2×
“However, we note that neutralization assays may underestimate the contribution of NTD-specific or non-RBM RBD-targeted neutralizing Abs (Lempp et al., 2021; McCallum et al., 2021a; Suryadevara et al., 2021), and protection from challenge will be the ultimate readout.”
Quadrivalent influenza nanoparticle vaccines induce broad protection
Boyoglu-Barnum, S., Ellis, D., Gillespie, R. A., Hutchinson, G. B., Park, Y., Moin, S. M., Acton, O. J., Ravichandran, R., Murphy, M., Pettie, D., et al. (2021) · Nature · doi:10.1038/s41586-021-03365-x · Cited by 326 · cited 2×
“, 2021b) and recent results obtained with influenza virus hemagglutinin nanoparticle vaccines (Boyoglu-Barnum et al., 2021).”
Self-citationNeutralization of SARS-CoV-2 by Destruction of the Prefusion Spike
Huo, J., Zhao, Y., Ren, J., Zhou, D., Duyvesteyn, H. M. E., Ginn, H. M., Carrique, L., Malinauskas, T., Ruza, R. R., Shah, P. N. M., et al. (2020) · Cell Host & Microbe · doi:10.1016/j.chom.2020.06.010 · Cited by 321
Adjuvanting a subunit COVID-19 vaccine to induce protective immunity
Arunachalam, P. S., Walls, A. C., Golden, N., Atyeo, C. G., Fischinger, S., Li, C., Aye, P. P., Navarro, M. J., Lai, L., Edara, V. V., et al. (2021) · Nature · doi:10.1038/s41586-021-03530-2 · Cited by 317 · cited 8×
“5 mg of AS03-adjuvanted prefusion-stabilized HexaPro S trimer (RBD EC50 1 3 10 (4)) and followed for 42 days (Arunachalam et al., 2021; Hsieh et al., 2020), as well as a panel of COVID-19 HCP (Table S2) (RBD EC50 2 3 10 (4)) (Figures 2A and S2A).”
InfluentialSelf-citationBroad and potent activity against SARS-like viruses by an engineered human monoclonal antibody
Rappazzo, C. G., Tse, L. V., Kaku, C. I., Wrapp, D., Sakharkar, M., Huang, D., Deveau, L. M., Yockachonis, T. J., Herbert, A. S., Battles, M. B., et al. (2021) · Science · doi:10.1126/science.abf4830 · Cited by 307 · cited 1×
“The isolation of RBD-specific cross-reactive mAbs neutralizing SARS-CoV-2 and SARS-CoV suggests that RBD-based vaccines could, in principle, elicit Abs that neutralize distantly related sarbecoviruses, which have future pandemic potential (Cathcart et al., 2021; Jette et al., 2021; Martinez et al., 2021a; Pinto et al.…”
Self-citationLectins enhance SARS-CoV-2 infection and influence neutralizing antibodies
Lempp, F. A., Soriaga, L. B., Montiel-Ruiz, M., Benigni, F., Noack, J., Park, Y., Bianchi, S., Walls, A. C., Bowen, J. E., Zhou, J., et al. (2021) · Nature · doi:10.1038/s41586-021-03925-1 · Cited by 305
Self-citationMosaic nanoparticle display of diverse influenza virus hemagglutinins elicits broad B cell responses
Kanekiyo, M., Joyce, M. G., Gillespie, R. A., Gallagher, J. R., Andrews, S. F., Yassine, H. M., Wheatley, A. K., Fisher, B. E., Ambrozak, D. R., Creanga, A., et al. (2019) · Nature Immunology · doi:10.1038/s41590-018-0305-x · Cited by 297 · cited 1×
“5438 Cell 184, 5432–5447, October 14, 2021 Design, assembly, and characterization of mosaic and cocktail sarbecovirus RBD-NPs We and others have recently evaluated nanoparticle immunogens that display multiple antigenic variants of viral glycoproteins as a potential route toward broadly protective vaccines (Boyoglu-Ba…”
Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail
Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00972-2 · Cited by 285
Self-citationAbu Jabal, K., Ben-Amram, H., Beiruti, K., Batheesh, Y., Sussan, C., Zarka, S., & Edelstein, M. (2021) · Eurosurveillance · doi:10.2807/1560-7917.es.2021.26.6.2100096 · Cited by 271
Ad26 vaccine protects against SARS-CoV-2 severe clinical disease in hamsters
Tostanoski, L. H., Wegmann, F., Martinot, A. J., Loos, C., McMahan, K., Mercado, N. B., Yu, J., Chan, C. N., Bondoc, S., Starke, C. E., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1070-6 · Cited by 270 · cited 1×
“As a result, SARS-CoV-2 S is the focus of nucleic acid, vectored, and protein subunit vaccines currently being developed and deployed (Corbett et al., 2020a, 2020b; Jackson et al., 2020; Mercado et al., 2020; Polack et al., 2020; Tostanoski et al., 2020; Yu et al., 2020).”
Broad sarbecovirus neutralization by a human monoclonal antibody
Tortorici, M. A., Czudnochowski, N., Starr, T. N., Marzi, R., Walls, A. C., Zatta, F., Bowen, J. E., Jaconi, S., di Iulio, J., Wang, Z., et al. (2021) · Nature · doi:10.1038/s41586-021-03817-4 · Cited by 255 · cited 2×
“5 3 10(1)) (Figures 2D and 2E; Data S1), which comprise conserved sarbecovirus epitopes recognized by broadly neutralizing sarbecovirus mAbs such as S2X259 (site II) and S309 (site IV) (Piccoli et al., 2020; Pinto et al., 2020; Tortorici et al., 2021).”
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
Self-citationInferring the shape of global epistasis
Otwinowski, J., McCandlish, D. M., & Plotkin, J. B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804015115 · Cited by 243 · cited 1×
“We next deconvolved variant-level escape scores into escape fraction estimates for singlemutations using global epistasismodels (Otwinowski et al., 2018) implemented in the dms_variants package, as detailed at (https://jbloomlab.”
Cathcart, A. L., Havenar‐Daughton, C., Lempp, F. A., Ma, D., Schmid, M., Agostini, M. L., Guarino, B., di Iulio, J., Rosen, L. E., Tucker, H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.09.434607 · Cited by 210 · cited 2×
“As a result, formulation of mAb cocktails or the use of mAbs targeting conserved epitopes and neutralizing a broader spectrum of circulating SARS-CoV-2 variants emerged as a promising strategy to overcome this issue (Baum et al., 2020b; Cathcart et al., 2021; Dong et al., 2021; Greaney et al., 2020; Jette et al., 2021…”
BackgroundSelf-citationStructural basis for broad coronavirus neutralization
Sauer, M. M., Tortorici, M. A., Park, Y., Walls, A. C., Homad, L. J., Acton, O. J., Bowen, J. E., Wang, C., Xiong, X., de van der Schueren, W., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00596-4 · Cited by 175 · cited 2×
“Although the S fusion machinery (S2 subunit) has higher sequence conservation than the RBD (Pinto et al., 2021; Sauer et al., 2021; Tortorici and Veesler, 2019; Walls et al., 2016, 2020a), the breadth of neutralization and protection provided by RBD-based vaccines remains unknown.”
Self-citationChimeric spike mRNA vaccines protect against Sarbecovirus challenge in mice
Martinez, D. R., Schäfer, A., Leist, S. R., la Cruz, G. D., West, A., Atochina‐Vasserman, E. N., Lindesmith, L. C., Pardi, N., Parks, R., Barr, M., et al. (2021) · Science · doi:10.1126/science.abi4506 · Cited by 175
Self-citationRockx, B., Corti, D., Donaldson, E., Sheahan, T., Stadler, K., Lanzavecchia, A., & Baric, R. (2008) · Journal of Virology · doi:10.1128/jvi.02377-07 · Cited by 134 · cited 8×
“REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies CR3022 ter Meulen et al., 2006 N/A S309 Pinto et al., 2020 N/A S2X259 Tortorici et al., 2021 N/A S2H14 Piccoli et al., 2020 N/A S230 Rockx et al., 2008 N/A Goat anti-mouse HRP Invitrogen Cat #626520; Lot #TG275230; AB_2533947 Goat anti-human HRP Invitrogen Cat #A18817;…”
InfluentialSelf-citationKrammer, F., Srivastava, K., the PARIS team, & Simon, V. (2021) · doi:10.1101/2021.01.29.21250653 · Cited by 116 · cited 2×
“We show that receiving a third immunization, even of an unaltered vaccine, improves the neutralizing Ab responses to VOCs, which is reminiscent of what has been shown in vaccinated humans previously infected with SARS-CoV-2 (Abu Jabal et al., 2021; Krammer et al., 2021; Stamatatos et al., 2021), suggesting that furthe…”
Jette, 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
Murine Leukemia Virus (MLV)-based Coronavirus Spike-pseudotyped Particle Production and Infection
Millet, J., & Whittaker, G. (2016) · BIO-PROTOCOL · doi:10.21769/bioprotoc.2035 · Cited by 91 · cited 2×
“Pseudovirus production MLV-based D614G SARS-CoV-2 S and SARS-CoV S pseudotypes were prepared as previously described (Millet and Whittaker, 2016; Walls et al., 2020a, 2020b).”
Cohen, A. A., Yang, Z., Gnanapragasam, P. N. P., Ou, S. K.-H., Dam, K.-M. A., Wang, H., & Björkman, P. J. (2021) · PLoS ONE · doi:10.1371/journal.pone.0247963 · Cited by 83
Kaname, Y., Tani, H., Kataoka, C., Shiokawa, M., Taguwa, S., Abe, T., Moriishi, K., Kinoshita, T., & Matsuura, Y. (2010) · Journal of Virology · doi:10.1128/jvi.02519-09 · Cited by 65
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
Self-citationMartinez, D. R., Schaefer, A., Gobeil, S., Li, D., la Cruz, G. D., Parks, R., Lu, X., Barr, M., Manne, K., Mansouri, K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.27.441655 · Cited by 37
Self-citationBoyoglu-Barnum, S., Ellis, D., Gillespie, R. A., Hutchinson, G. B., Park, Y., Moin, S. M., Acton, O. J., Ravichandran, R., Murphy, M., Pettie, D., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.30.125179 · Cited by 32
Self-citationLempp, F., Soriaga, L. B., Montiel-Ruiz, M., Benigni, F., Noack, J., Park, Y.-J., Bianchi, S., Walls, A., Bowen, J., Zhou, J.-Y., et al. (2021) · bioRxiv · doi:10.1101/2021.04.03.438258 · Cited by 22 · cited 2×
“However, we note that neutralization assays may underestimate the contribution of NTD-specific or non-RBM RBD-targeted neutralizing Abs (Lempp et al., 2021; McCallum et al., 2021a; Suryadevara et al., 2021), and protection from challenge will be the ultimate readout.”
Self-citationAn Engineered Antibody with Broad Protective Efficacy in Murine Models of SARS and COVID-19Preprint
Rappazzo, C. G., Tse, L. V., Kaku, C. I., Wrapp, D., Sakharkar, M., Huang, D., Deveau, L. M., Yockachonis, T. J., Herbert, A. S., Battles, M. B., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.17.385500 · Cited by 16
Self-citationArunachalam, P. S., Walls, A. C., Golden, N., Atyeo, C. G., Fischinger, S., Li, C., Aye, P. P., Navarro, M. J., Lai, L., Edara, V. V., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.10.430696 · Cited by 15
Self-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 4×
“To understand the impact of the full constellation of mutations present in the S proteins of the aforementioned VOCs, we evaluated RBD-NP- andHexaPro S-elicited serum neutralizing activity against corresponding HIV and VSV pseudotyped variants (D614G GMT RBD-NP HIV 5 3 103 and VSV RBD-NP 6 3 102, respectively, and D61…”
BackgroundInfluentialSelf-citationSARS-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
Flagged first, then by citations
Research works printed but not linked: 1
- Davies, 2020, Estimated transmissibility and severity of novel SARS-CoV-2 Variant of Concern 202012/01 in England, medRxiv
Cited by
Sorted by citations
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift
Cameroni, E., Bowen, J. E., Rosen, L. E., Saliba, C., Zepeda, S. K., Culap, K., Pinto, D., VanBlargan, L. A., Marco, A. D., di Iulio, J., et al. (2021) · Nature · doi:10.1038/s41586-021-04386-2 · Cited by 1,070
Self-citationStructural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement
McCallum, M., Czudnochowski, N., Rosen, L. E., Zepeda, S. K., Bowen, J. E., Walls, A. C., Hauser, K., Joshi, A., Stewart, C., Dillen, J. R., et al. (2022) · Science · doi:10.1126/science.abn8652 · Cited by 535
“The identification of broadly reactive mAbs that neutralize multiple distinct sarbecoviruses, including SARS-CoV-2 variants, pave the way for designing vaccines eliciting broad sarbecovirus immunity ( 52 – 56 ).”
Self-citationSARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Starr, T. N., Czudnochowski, N., Liu, Z., Zatta, F., Park, Y., Addetia, A., Pinto, D., Beltramello, M., Hernandez, P., Greaney, A. J., et al. (2021) · Nature · doi:10.1038/s41586-021-03807-6 · Cited by 503
Self-citationBroad betacoronavirus neutralization by a stem helix–specific human antibody
Pinto, D., Sauer, M. M., Czudnochowski, N., Low, J. S., Tortorici, M. A., Housley, M. P., Noack, J., Walls, A. C., Bowen, J. E., Guarino, B., et al. (2021) · Science · doi:10.1126/science.abj3321 · Cited by 385
Self-citationUnadjuvanted intranasal spike vaccine elicits protective mucosal immunity against sarbecoviruses
Mao, T., Israelow, B., Peña-Hernández, M. A., Suberi, A., Zhou, L., Luyten, S., Reschke, M., Dong, H., Homer, R., Saltzman, W. M., et al. (2022) · Science · doi:10.1126/science.abo2523 · Cited by 356
“Although some recent studies have successfully reported the development of systemic pan-sarbecovirus vaccines (37, 38), P&Sx induces both systemic andmucosal immunity against both SARS-CoV-1 and SARS-CoV-2.”
Result
Metadata
- Authors
- Walls, A. C., Miranda, M. C., Schäfer, A., Pham, M. N., Greaney, A., Arunachalam, P. S., Navarro, M.-J., Tortorici, M. A., Rogers, K., O’Connor, M. A., Shirreff, L., Ferrell, D. E., Bowen, J., Brunette, N., Kepl, E., Zepeda, S. K., Starr, T., Hsieh, C.-L., Fiala, B., Wrenn, S., Pettie, D., Sydeman, C., Sprouse, K. R., Johnson, M., Blackstone, A., Ravichandran, R., Ogohara, C., Carter, L., Tilles, S. W., Rappuoli, R., Leist, S. R., Martinez, D. R., Clark, M., Tisch, R., O’Hagan, D. T., Van Der Most, R., Van Voorhis, W. C., Corti, D., McLellan, J. S., Kleanthous, H., Sheahan, T. P., Smith, K. D., Fuller, D. H., Villinger, F., Bloom, J., Pulendran, B., Baric, R. S., King, N. P., & Veesler, D.
- Affiliations
- University of Washington (US)
- University of North Carolina at Chapel Hill (US)
- Stanford University (US)
- Centre National de la Recherche Scientifique (FR)
- University of Louisiana at Lafayette (US)
- Fred Hutch Cancer Center (US)
- The University of Texas at Austin (US)
- GlaxoSmithKline (Italy) (IT)
- Vir Biotechnology (Switzerland) (CH)
- Gates Foundation (US)
- Corresponding author
- King, Neil P.
- Veesler, David
- ORCID
- Walls, Alexandra C.
- Miranda, Marcos C.
- Schäfer, Alexandra
- Pham, Minh N.
- Greaney, Allison
- Arunachalam, Prabhu S.
- Navarro, Mary-Jane
- Tortorici, M. Alejandra
- Rogers, Kenneth
- O’Connor, Megan A.
- Shirreff, Lisa
- Ferrell, Douglas E.
- Bowen, John
- Brunette, Natalie
- Kepl, Elizabeth
- Zepeda, Samantha K.
- Starr, Tyler
- Hsieh, Ching-Lin
- Fiala, Brooke
- Wrenn, Samuel
- Pettie, Deleah
- Sprouse, Kaitlin R.
- Johnson, Max
- Ravichandran, Rashmi
- Carter, Lauren
- Tilles, Sasha W.
- Rappuoli, Rino
- Leist, Sarah R.
- Martinez, David R.
- Clark, Matthew
- Tisch, Roland
- Corti, Davide
- McLellan, Jason S.
- Kleanthous, Harry
- Sheahan, Timothy P.
- Smith, Kelly D.
- Fuller, Deborah H.
- Villinger, Francois
- Bloom, Jesse
- Pulendran, Bali
- Baric, Ralph S.
- King, Neil P.
- Veesler, David
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-10
- Volume
- 184
- Issue
- 21
- Pages
- 5432-5447.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7986998
- OpenAlex
- W3199882158
- Cited by
- 185
- References
- 116
- Citations by year
- 2026: 15 · 2025: 24 · 2024: 27 · 2023: 35 · 2022: 59 · 2021: 25
- FWCI
- 11.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 378 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- Burroughs Wellcome Fund (U01 AI149644, HHSN272201700036I-75N93020F00001)
- Howard Hughes Medical Institute
- Defense Threat Reduction Agency (HDTRA1-18-1-0001)
- National Institute of General Medical Sciences (R01GM120553)
- Bill and Melinda Gates Foundation (017592, OPP1156262, INV\u2013017592)
- Pfizer
- University of Washington
- Gilead Sciences
- GlaxoSmithKline (63/032,502)
- North Carolina General Assembly
- National Institute of Allergy and Infectious Diseases (DP1AI158186, F32 AI152296, T32 AI007151, R01-AI127521, 5T32GM008268-32, HHSN272201700059C)
- Office of Research Infrastructure Programs, National Institutes of Health (P51-OD010425)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- Sarbecovirus, SARS-CoV-2, receptor binding domain, nanoparticle vaccine, multivalent vaccine, heterologous protection, neutralizing antibodies, SARS-CoV, spike protein mutations, mosaic vaccine, dose sparing, non-human primates
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.
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