N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
Open accessPreprint — published as 10.1016/j.cell.2021.03.028 · Paper page
Abstract
SARS-CoV-2 entry into host cells is orchestrated by the spike (S) glycoprotein that contains an immunodominant receptor-binding domain (RBD) targeted by the largest fraction of neutralizing antibodies (Abs) in COVID-19 patient plasma. Little is known about neutralizing Abs binding to epitopes outside the RBD and their contribution to protection. Here, we describe 41 human monoclonal Abs (mAbs) derived from memory B cells, which recognize the SARS-CoV-2 S N-terminal domain (NTD) and show that a subset of them neutralize SARS-CoV-2 ultrapotently. We define an antigenic map of the SARS-CoV-2 NTD and identify a supersite recognized by all known NTD-specific neutralizing mAbs. These mAbs inhibit cell-to-cell fusion, activate effector functions, and protect Syrian hamsters from SARS-CoV-2 challenge. SARS-CoV-2 variants, including the 501Y.V2 and B.1.1.7 lineages, harbor frequent mutations localized in the NTD supersite suggesting ongoing selective pressure and the importance of NTD-specific neutralizing mAbs to protective immunity.
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Neutralizing mAbs that bind regions of the viral spike have also been identified.
“Neutralizing mAbs that bind regions of the viral spike have also been identified (24, 33, 38–42).”
From mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection (2021) · cites this paper as [39]
In older adults mean GMT was only 12 in a preliminary analysis of 12 participants and increased to 109 after the second dose.
“In older adults mean GMT was only 12 in a preliminary analysis of 12 participants19 and increased to 109 after the second dose.”
From Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies (2021) · cites this paper as [19]
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“, 2021), the in vitro selection of SARS-CoV-2 S escape variants with NTD mutations that decrease the neutralization potency of COVID-19 convalescent patient sera (Andreano et al., 2020; Weisblum et al., 2020), and the escape mutants reported here.”
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“Binding at this so-called ‘‘supersite’’ has been reported as of potential therapeutic relevance (McCallum et al., 2021).”
BackgroundSARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
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Self-citationSARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
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Self-citationEscape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
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Self-citationmRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection
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SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
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Self-citationSpread of a SARS-CoV-2 variant through Europe in the summer of 2020
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Self-citationRecurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the Alpha variant B.1.1.7
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“DeletionsinotherpartsoftheN-terminal domain (NTD) have been reported to arise in chronic infection (Choi et al., 2020) and reduce sensitivity to NTD-specific neutralizing antibodies (McCallum et al., 2021; McCarthy et al., 2021).”
Self-citationSuryadevara, 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 397 · see citing works
“There is only limited precedence for in vivo protection against SARS-CoV-2 infection or disease mediated by mAbs that react to S protein regions outside the RBD (McCallum et al., 2021; Voss et al., 2020; Zhang et al., 2020).”
Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron
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“The NTD-1 epitope overlaps with that of mAb 4A8 ( 27 ) and other “supersite” binders ( 28 , 29 ).”
BackgroundChatterjee, S., Bhattacharya, M., Nag, S., Dhama, K., & Chakraborty, C. (2023) · Viruses · doi:10.3390/v15010167 · Cited by 313 · see citing works
Lectins enhance SARS-CoV-2 infection and influence neutralizing antibodies
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Self-citationImpact of circulating SARS-CoV-2 variants on mRNA vaccine-induced immunity
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“Although the RBD is immunodominant, there is evidence for a substantial role of other spike regions in antigenicity, most notably the NTD supersite 22–24 .”
BackgroundSARS-CoV-2 prolonged infection during advanced HIV disease evolves extensive immune escape
Cele, S., Karim, F., Lustig, G., San, J. E., Hermanus, T., Tegally, H., Snyman, J., Moyo-Gwete, T., Wilkinson, E., Bernstein, M. P., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2022.01.005 · Cited by 230 · see citing works
“Mutations associated with neutralization escape are found in the receptor-binding domain (RBD) (Barnes et al., 2020, Greaney et al., 2021a, Greaney et al., 2021b) and N-terminal domain of the spike (McCallum et al., 2021, Cerutti et al., 2021, Suryadevara et al., 2021, Chi et al., 2020).”
Immune responses to two and three doses of the BNT162b2 mRNA vaccine in adults with solid tumors
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High genetic barrier to SARS-CoV-2 polyclonal neutralizing antibody escape
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Chimeric spike mRNA vaccines protect against Sarbecovirus challenge in mice
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SARS-CoV-2 breakthrough infections elicit potent, broad, and durable neutralizing antibody responses
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“…S2P trimer GeneArt N/A SARS-CoV-2 S full-length D614G (YP 009724390.1) Crawford et al., 2020 Vector# BEI NR-52514 SARS-CoV-2 Delta GenScript (McCallum et al., 2021a) N/A SARS-CoV-2 Beta GenScript (Cameroni et al., 2021) Vector# BEI NR-52517 SARS-CoV-2 Omicron Cameroni et al., 2021 Vector#…”
InfluentialSelf-citationWillett, B., Grove, J., MacLean, O., et al. (2022) · medRxiv · doi:10.1101/2022.01.03.21268111 · Cited by 182 · see citing works
Structural Diversity of the SARS-CoV-2 Omicron Spike
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“1 that targets a site of vulnerability in the NTD ( 20, 24 ), no longer bound the Delta and Omicron S proteins (Fig.”
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
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A pseudovirus system enables deep mutational scanning of the full SARS-CoV-2 spike
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“NTD and is one of the few NTD-targeting antibodies isolated pre-Omicron that still retains some potency against Omicron variants.(2,33,38) The deep mutational scanning showed that the key escape sites for 5-7 were in a hydrophobic pocket next to the N4 loop (site 172-178) (Figure 5A-C and https://dms-vep.”
The humoral response and antibodies against SARS-CoV-2 infection
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Self-citationEffects of SARS-CoV-2 variants on vaccine efficacy and response strategies
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“[16,39] or in the ACE2-binding site, which is a major target of potent virus-neutralizing antibodies [7,33].”
BackgroundSARS-CoV-2 one year on: evidence for ongoing viral adaptation
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“The NTD can also be recognized by antibodies, and some antibodies targeting the NTD potentially neutralize viral infection (Lok, 2021; Voss et al., 2021; Cerutti et al., 2021; Suryadevara et al., 2021; McCallum et al., 2021; Liu et al., 2020; Chi et al., 2020), despite our limited understanding of its virological func…”
Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma
Cele, S., Gazy, I., Jackson, L., Hwa, S.-H., Tegally, H., Lustig, G., Giandhari, J., Pillay, S., Wilkinson, E., Naidoo, Y., et al. (2021) · doi:10.1101/2021.01.26.21250224 · Cited by 651 · see citing works
“NAbs targeting this site have been shown to be potent neutralizers of SARS-CoV-2 [5, 6].”
BackgroundImprinted SARS-CoV-2 humoral immunity induces convergent Omicron RBD evolution
Cao, Y., Jian, F., Wang, J., Yu, Y., Song, W., Yisimayi, A., Wang, J., An, R., Chen, X., Zhang, N., et al. (2022) · Nature · doi:10.1038/s41586-022-05644-7 · Cited by 801 · see citing works
Planas, D., Veyer, D. L., Baidaliuk, A., Staropoli, I., Guivel‐Benhassine, F., Rajah, M. M., Planchais, C., Porrot, F., Robillard, N., Puech, J., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.26.445838 · Cited by 272 · see citing works
Scientific rationale for developing potent RBD-based vaccines targeting COVID-19
Kleanthous, H., Silverman, J., Makar, K., Yoon, I., Jackson, N. A. C., & Vaughn, D. (2021) · npj Vaccines · doi:10.1038/s41541-021-00393-6 · Cited by 137 · see citing works
SARS-CoV-2 immune evasion by variant B.1.427/B.1.429Preprint
McCallum, M., Bassi, J., Marco, A. D., Chen, A., Walls, A. C., di Iulio, J., Tortorici, M. A., Navarro, M.-J., Silacci-Fregni, C., Saliba, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437925 · Cited by 128 · see citing works
Self-citationEvolutionary trajectory of SARS-CoV-2 and emerging variants
Singh, J., Pandit, P., McArthur, A. G., Banerjee, A., & Mossman, K. L. (2021) · Virology Journal · doi:10.1186/s12985-021-01633-w · Cited by 144 · see citing works
Antibody-mediated neutralization of SARS-CoV-2
Gruell, H., Vanshylla, K., Weber, T., Barnes, C. O., Kreer, C., & Klein, F. (2022) · Immunity · doi:10.1016/j.immuni.2022.05.005 · Cited by 145 · see citing works
Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galão, R. P., Dupont, L., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.03.023 · Cited by 130 · see citing works
“The D Y144 deletion, which has a prevalence of 1.7% in 37 countries (McCallum et al., 2021), has been shown to abrogate binding to other NTD mAbs including S2M28, S2X28, S2X333, and 4A8 (Chi et al., 2020; McCallum et al., 2021).”
InfluentialWang, Z., Muecksch, F., Cho, A., Gaebler, C., Hoffmann, H.-H., Ramos, V., Zong, S., Cipolla, M., Johnson, B., Schmidt, F., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.04.003 · Cited by 142 · see citing works
“…supersite consisting of variable loops flanked by glycans (Amanat et al., 2021; Cerutti et al., 2021b; Chi et al., 2020; Dussupt et al., 2021; Haslwanter et al., 2021; Li et al., 2021; Liu et al., 2021; McCallum et al., 2021a; Planas et al., 2021b; Suryadevara et al., 2021b; Voss et al., 2021).”
InfluentialNeutralizing antibodies for the prevention and treatment of COVID-19
Du, L., Yang, Y., & Zhang, X. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00752-2 · Cited by 120 · see citing works
Characterizations of enhanced infectivity and antibody evasion of Omicron BA.2.75
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The SARS-CoV-2 Lambda variant exhibits enhanced infectivity and immune resistance
Kimura, I., Kosugi, Y., Wu, J., Zahradník, J., Yamasoba, D., Butlertanaka, E. P., Tanaka, Y., Uriu, K., Liu, Y., Morizako, N., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110218 · Cited by 210 · see citing works
“In addition, mutations in the N-terminal domain (NTD) of the SARSCoV-2 S protein are associated with neutralization escape (McCallum et al., 2021).”
Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New York
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) · Nature Communications · doi:10.1038/s41467-021-25168-4 · Cited by 130 · see citing works
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Recurrent SARS-CoV-2 mutations in immunodeficient patients
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“Two occurrences of S:Δ243, another NTD supersite mutation, were also observed, another deletion that has been demonstrated to decrease Ab neutralisation in vitro (McCarthy et al. 2021; McCallum et al. 2021b).”
BackgroundBeaudoin-Bussières, G., Chen, Y., Ullah, I., Prévost, J., Tolbert, W. D., Symmes, K., Ding, S., Benlarbi, M., Gong, S. Y., Tauzin, A., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110368 · Cited by 120 · see citing works
“…nAbs whose structures have been determined recognized a similar glycan-free epitope (Cerutti et al., 2021; Chi et al., 2020; Liu et al., 2020; McCallum et al., 2021; Sun et al., 2021; Voss et al., 2021), named the NTD supersite (residues 14–20, 140–158, and 245–264) (Harvey et al., 2021;…”
BackgroundMethodInfluentialMutations of SARS-CoV-2 spike protein: Implications on immune evasion and vaccine-induced immunity
Mengist, H. M., Kombe, A. J. K., Mekonnen, D., Abebaw, A., Getachew, M., & Jin, T.-C. (2021) · Seminars in Immunology · doi:10.1016/j.smim.2021.101533 · Cited by 114 · see citing works
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Cerutti, G., Guo, Y., Liu, L., Liu, L., Zhang, Z., Luo, Y., Huang, Y., Wang, H. H., Ho, D. D., Sheng, Z., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110428 · Cited by 104 · see citing works
“…et al., 2021c; Chen et al., 2020; Ju et al., 2020; Liu et al., 2020b; Pinto et al., 2020; Rapp et al., 2021; Shi et al., 2020; Tortorici et al., 2020; Zost et al., 2020), and N-terminal domain (NTD) (Cerutti et al., 2021a, 2021b; Chi et al., 2020;McCallum et al., 2021a; Suryadevara et al., 2021).”
BackgroundTherapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies
Zhou, Y., Xie, Y., Tang, L., Pu, D., Zhu, Y., Liu, J., & Ma, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00733-x · Cited by 115 · see citing works
“All 144 and 242–244 deletions and R246I fall within the supersite of NTD.120,121 P.1 does not have NTD deletions but NTD mutations (R190S, D138Y, P26S, T20N, and L18F), which could influence the binding of mAbs.”
BackgroundInfluentialThe global epidemic of SARS‐CoV‐2 variants and their mutational immune escape
Tian, D., Sun, Y., Zhou, J., & Ye, Q. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27376 · Cited by 101 · see citing works
“7 pseudovirus to escape the neutralization of mAbs (4A8, S2X28, S2M28, and S2X333).(73) Another study showed that the B.”
BackgroundSelf-citationCho, H., Gonzales-Wartz, K. K., Huang, D.-L., Yuan, M., Peterson, M., Liang, J. Y., Beutler, N., Torres, J., Cong, Y., Postnikova, E., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj5413 · Cited by 109 · see citing works
SARS-CoV-2 spike protein: pathogenesis, vaccines, and potential therapies
Almehdi, A. M., Khoder, G., Alchakee, A., Alsayyid, A. T., Sarg, N. H., & Soliman, S. S. M. (2021) · Infection · doi:10.1007/s15010-021-01677-8 · Cited by 113 · see citing works
“On the other hand, 41 human monoclonal Abs (mAbs) derived from memory B cells have been identified and showed potent neutralizing activity against SARS-CoV-2 S N-terminal domain (NTD), specifically supersite I, suggesting its importance for protective immunity and vaccine design [70].”
BackgroundStamatatos, 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) · doi:10.1101/2021.02.05.21251182 · Cited by 559 · see citing works
“Neutralizing mAbs targeting epitopes on the NTD of S1 (24, 34, 38-40) and S2 have also been identified (41, 42).”
BackgroundCryo-EM structures of SARS-CoV-2 Omicron BA.2 spike
Stalls, V., Lindenberger, J. J., Gobeil, S., Henderson, R. C., Parks, R., Barr, M., Deyton, M., Martin, M., Janowska, K., Huang, X., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111009 · Cited by 101 · see citing works
Li, W., Chen, Y., Prévost, J., Ullah, I., Lu, M., Gong, S. Y., Tauzin, A., Gasser, R., Vézina, D., Anand, S. P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110210 · Cited by 125 · see citing works
“…antibodies have been identified (Hoffmann et al., 2020; Jennewein et al., 2021; Jette et al., 2021; Li et al., 2021b; Ma et al., 2020; Ng et al., 2020; Rap-pazzo et al., 2021; Song et al., 2021; Tian et al., 2020; Tortorici et al., 2021; Wang et al., 2020, 2021a; Wec Anna et al., 2020).”
Tortorici, M. A., Walls, A. C., Joshi, A., Park, Y., Eguia, R. T., Miranda, M. C., Kepl, E., Dosey, A. M., Stevens‐Ayers, T., Boeckh, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.019 · Cited by 87 · see citing works
“…immune evasion, replication kinetics or disease severity relative to the ancestral SARS-CoV-2 isolate (Cele et al., 2021; Collier et al., 2021; Davies et al., 2021; Edara et al., 2021; Liu et al., 2021a, 2021b; McCallum et al., 2021a, 2021b; Plante et al., 2020; Wibmer et al., 2021).”
Self-citationSignatures in SARS-CoV-2 spike protein conferring escape to neutralizing antibodies
Alenquer, M., Ferreira, F., Lousa, D., Valério, M., Medina-Lopes, M., Bergman, M., Gonçalves, J., Demengeot, J., Leite, R. B., Lilue, J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009772 · Cited by 99 · see citing works
“All the antibodies analyzed are neutralizing antibodies, which is not the case in nature [54].”
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Self-citationStructural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit
Hurlburt, N. K., Homad, L. J., Sinha, I. R., Jennewein, M. F., MacCamy, A. J., Wan, Y.-H., Boonyaratanakornkit, J. B., Sholukh, A. M., Jackson, A. M., Zhou, P.-P., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03262-7 · Cited by 77 · see citing works
“The neutralizing potency of CV3-25 is not affected by mutations found in SARS-CoV-2 variants of concern, which harbor mutations that escape from many anti-NTD and anti-RBD antibodies.”
BackgroundInfluentialMannar, D., Saville, J. W., Zhu, X. Q., Srivastava, S. S., Berezuk, A., Zhou, S., Tuttle, K. S., Kim, A., Li, W., Dimitrov, D. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110156 · Cited by 88 · see citing works
“Although we have focused the present study on RBD mutations present within VoCs, it is possible that mutations elsewhere in the S protein (particularly in the N-terminal domain) also play a significant role in antibody evasion and may affect ACE2 binding (McCallum et al., 2021).”
InfluentialTackling COVID-19 with neutralizing monoclonal antibodies
Corti, D., Purcell, L. A., Snell, G., & Veesler, D. (2021) · Cell · doi:10.1016/j.cell.2021.07.027 · Cited by 78 · see citing works
“…Cell 184, June 10, 2021 bodies, possibly reducing vaccine effectiveness and the duration of protection (Cele et al., 2021; Chen et al., 2021c; Collier et al., 2021; Kustin et al., 2021; Liu et al., 2021a; McCallum et al., 2021a; Muik et al., 2021; Wang et al., 2021b, 2021c; Wu et al., 2021).”
InfluentialSelf-citationSaville, J. W., Mannar, D., Zhu, X. Q., Srivastava, S. S., Berezuk, A., Demers, J., Zhou, S., Tuttle, K. S., Sekirov, I., Kim, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28324-6 · Cited by 93 · see citing works
Bianchini, F., Crivelli, V., Abernathy, M. E., Guerra, C., Palus, M., Muri, J., Marcotte, H., Piralla, A., Pedotti, M., Gasparo, R. D., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.ade0958 · Cited by 83 · see citing works
A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy
Greaney, A. J., Starr, T. N., Eguia, R. T., Loes, A. N., Khan, K., Karim, F., Cele, S., Bowen, J., Logue, J. K., Corti, D., et al. (2021) · bioRxiv · doi:10.1371/journal.ppat.1010248 · Cited by 71 · see citing works
Self-citationSun, S., He, L., Zhao, Z., Gu, H., Fang, X. D., Wang, T., Yang, X., Chen, S., Deng, Y., Li, J., et al. (2021) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00658-z · Cited by 71 · see citing works
Venkatakrishnan, A., Anand, P., Lenehan, P. J., Suratekar, R., Raghunathan, B., Niesen, M. J. M., & Soundararajan, V. (2021) · doi:10.31219/osf.io/f7txy · Cited by 58 · see citing works
Dussupt, V., Sankhala, R., Mendez-Rivera, L., Townsley, S. M., Schmidt, F., Wieczorek, L., Lal, K. G., Donofrio, G., Tran, U., Jackson, N. D., et al. (2021) · Nature Immunology · doi:10.1038/s41590-021-01068-z · Cited by 66 · see citing works
An overview of the vaccine platforms to combat COVID-19 with a focus on the subunit vaccines
Bayani, F., Hashkavaei, N. S., Arjmand, S., Rezaei, S., Uskoković, V., Alijanianzadeh, M., Uversky, V. N., Siadat, S. O. R., Mozaffari‐Jovin, S., & Sefidbakht, Y. (2023) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2023.02.004 · Cited by 63 · see citing works
Cerutti, G., Guo, Y., Wang, P., Nair, M. S., Wang, M., Huang, Y., Yu, J., Liu, L., Katsamba, P. S., Bahna, F. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109928 · Cited by 63 · see citing works
“The basis for the restriction of potent neutralization to site 1 is unclear; however, preliminary studies are consistent with a conformational mechanism for supersite-directed antibodies in which membrane fusion is inhibited (McCallum et al., 2021b; Suryadevara et al., 2021).”
Dynamics of SARS-CoV-2 Spike Proteins in Cell Entry: Control Elements in the Amino-Terminal Domains
Qing, E., Kicmal, T., Kumar, B., Hawkins, G. M., Timm, E. C., Perlman, S. M., & Gallagher, T. (2021) · mBio · doi:10.1128/mbio.01590-21 · Cited by 67 · see citing works
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A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
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mRNA-1273 protects against SARS-CoV-2 beta infection in nonhuman primates
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Accelerated evolution of SARS-CoV-2 in free-ranging white-tailed deer
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Understanding the Secret of SARS-CoV-2 Variants of Concern/Interest and Immune Escape
Lou, F., Li, M., Pang, Z., Jiang, L., Guan, L., Tian, L., Hu, J., Fan, J., & Fan, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.744242 · Cited by 53 · see citing works
“In addition, the L18F mutation located in the NTD was shown to be related to immune escape potentiality (32).”
BackgroundSARS-CoV-2 spike N-terminal domain modulates TMPRSS2-dependent viral entry and fusogenicity
Meng, B., Datir, R. P., Choi, J., Baker, S. G., Dougan, G., Hess, C., Kingston, N., Lehner, P. J., Lyons, P., Matheson, N. J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111220 · Cited by 52 · see citing works
“Although Kappa, the earliest detected B.1.617 variant in India, displayed greater escape to vaccine-elicited antibody responses (McCallum et al., 2021a), Delta surpassed Kappa to become the dominant strain in India and worldwide by mid-2021 (Mlcochova et al., 2021).”
InfluentialTaylor, A. L., & Starr, T. N. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011901 · Cited by 57 · see citing works
“Therefore, the continued presence of affinity-enhancing mutations in the BQ.1.1 and XBB.1.5 landscapes will likely facilitate ongoing antigenic evolution via compensatory epistasis.”
BackgroundInfluential
- Authors
- McCallum, M., Marco, A. D., Lempp, F., Tortorici, M. A., Pinto, D., Walls, A. C., Beltramello, M., Chen, A., Liu, Z., Zatta, F., Zepeda, S., di Iulio, J., Bowen, J. E., Montiel-Ruiz, M., Zhou, J., Rosen, L. E., Bianchi, S., Guarino, B., Fregni, C. S., Abdelnabi, R., Caroline Foo, S.-Y., Rothlauf, P. W., Bloyet, L.-M., Benigni, F., Cameroni, E., Neyts, J., Riva, A., Snell, G., Telenti, A., Whelan, S. P. J., Virgin, H. W., Corti, D., Pizzuto, M. S., & Veesler, D.
- Affiliations
- University of Washington (US)
- Vir Biotechnology (Switzerland) (CH)
- VIR Biotechnology (United States) (US)
- Centre National de la Recherche Scientifique (FR)
- Washington University in St. Louis (US)
- Rega Institute for Medical Research (BE)
- University of Milan (IT)
- Corresponding author
- Corti, Davide
- Pizzuto, Matteo Samuele
- Veesler, David
- ORCID
- McCallum, Matthew
- Marco, Anna De
- Lempp, Florian
- Tortorici, M. Alejandra
- Pinto, Dora
- Walls, Alexandra C.
- Beltramello, Martina
- Chen, Alex
- Liu, Zhuoming
- Zatta, Fabrizia
- Zepeda, Samantha
- Bowen, John E.
- Montiel-Ruiz, Martin
- Zhou, Jiayi
- Rosen, Laura E.
- Bianchi, Siro
- Guarino, Barbara
- Abdelnabi, Rana
- Rothlauf, Paul W.
- Bloyet, Louis-Marie
- Benigni, Fabio
- Cameroni, Elisabetta
- Neyts, Johan
- Riva, Agostino
- Snell, Gyorgy
- Telenti, Amalio
- Whelan, Sean P.J.
- Virgin, Herbert W.
- Corti, Davide
- Pizzuto, Matteo Samuele
- Veesler, David
- Venue
- Cell
- Publisher
- openRxiv
- Published
- 2021-01-14
- Volume
- 184
- Issue
- 9
- Pages
- 2332-2347.e16
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7814825
- OpenAlex
- W3136616180
- Cited by
- 901
- References
- 0
- Citations by year
- 2026: 38 · 2025: 64 · 2024: 92 · 2023: 154 · 2022: 270 · 2021: 269 · 2020: 2 · 2018: 1 · 2017: 1 · 2015: 1 · 2014: 2 · 2013: 1
- FWCI
- 62.32
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Lirias (acceptedVersion, other-oa)
- PubMed Central (submittedVersion)
- HAL (submittedVersion)
- Archivio Istituzionale della Ricerca (Universita Degli Studi Di Milano) (submittedVersion, other-oa)
- Lirias (submittedVersion, other-oa)
- Funders
- Burroughs Wellcome Fund
- University of Washington
- Fast Grants
- National Institutes of Health (1s10od023476-01)
- Natural Sciences and Engineering Research Council of Canada (HHSN272201700059C)
- National Institute of General Medical Sciences (R01GM120553, T32GM008268)
- National Institute of Allergy and Infectious Diseases (HHSN272201700059C, DP1AI158186)
- 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, N-terminal domain, neutralizing antibodies, monoclonal antibodies, antigenic mapping, receptor binding domain, SARS-CoV-2 variants, Alpha variant, Beta variant, P.1 lineage, vaccine design
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