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SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern

Matthew McCallum, Jessica Bassi, Anna De Marco and 29 more

Science · 2021 · CC BY

doi:10.1126/science.abi7994

Abstract

SARS-CoV-2 from alpha to epsilon As battles to contain the COVID-19 pandemic continue, attention is focused on emerging variants of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus that have been deemed variants of concern because they are resistant to antibodies elicited by infection or vaccination or they increase transmissibility or disease severity. Three papers used functional and structural studies to explore how mutations in the viral spike protein affect its ability to infect host cells and to evade host immunity. Gobeil et al . looked at a variant spike protein involved in transmission between minks and humans, as well as the B1.1.7 (alpha), B.1.351 (beta), and P1 (gamma) spike variants; Cai et al . focused on the alpha and beta variants; and McCallum et al . discuss the properties of the spike protein from the B1.1.427/B.1.429 (epsilon) variant. Together, these papers show a balance among mutations that enhance stability, those that increase binding to the human receptor ACE2, and those that confer resistance to neutralizing antibodies. —VV

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 17, 2026. Paragraph numbers are ours, so an answer can point at one.

COVID-19 is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and is associated with acute respiratory distress syndrome, as well as extrapulmonary complications such as vascular thrombosis, coagulopathy, and a hyperinflammatory syndrome contributing to disease severity and mortality. SARS-CoV-2 infects target cells using the spike glycoprotein (S), which is organized as a homotrimer with each monomer comprising an S1 and an S2 subunit. The S1 subunit harbors the receptor-binding domain (RBD) and the N-terminal domain (NTD), as well as two other domains designated here as C and D. The RBD interacts with the angiotensin-converting enzyme 2 (ACE2) entry receptor on host cells through a subset of amino acids forming the receptor-binding motif. The NTD was suggested to bind DC-SIGN, L-SIGN, and AXL, which may act as attachment receptors. Both the RBD and the NTD are targeted by neutralizing antibodies (Abs) in infected or vaccinated individuals, and some RBD-specific monoclonal Abs (mAbs) are currently being evaluated in clinical trials or are authorized for use in COVID-19 patients. The S2 subunit is the fusion machinery that merges viral and host membranes to initiate infection and is the target of Abs cross-reacting with multiple coronavirus subgenera because of its higher sequence conservation compared with the S1 subunit.

The ongoing global spread of SARS-CoV-2 led to the fixation of the D614G substitution, as well as to the emergence of a large number of viral lineages worldwide, including several variants of concern (VOC). Specifically, the B.1.1.7, B.1.351, and P.1 lineages that originated in the United Kingdom, South Africa, and Brazil, respectively, are characterized by the accumulation of mutations in the S gene as well as in other genes. Some of these mutations lead to marked reductions in the neutralization potency of several mAbs, convalescent sera, and Pfizer/BioNTech BNT162b2– or Moderna mRNA-1273–elicited Abs. The B.1.1.7 variant has become dominant worldwide because of its higher transmissibility, underscoring the importance of studying and understanding the consequences of SARS-CoV-2 antigenic drift.

The incidence of the B.1.427/B.1.429 lineages is increasing rapidly

The SARS-CoV-2 B.1.427/B.1.429 variant was reported for the first time at the beginning of 2021 in California, and as of May 2021 had been detected in 34 additional countries. The two lineages B.1.427 and B.1.429 (belonging to clade 20C according to Nextstrain designation) share the same S mutations (S13I in the signal peptide, W152C in the NTD, and L452R in the RBD) but harbor different mutations in other SARS-CoV-2 genes. Molecular clock analysis suggested that the progenitor of both lineages emerged in May 2020, diverging to give rise to the B.1.427 and B.1.429 lineages in June and July 2020. The fast rise in the number of cases associated with the B.1.427/B.1.429 lineages led to their classification as a VOC by the US Centers for Disease Control and Prevention (https://www.cdc.gov/coronavirus/2019-ncov/cases-updates/variant-surveillance/variant-info.html).

As of 30 April 2021, 8441 and 21,072 sequenced genomes had been reported in GISAID (Global Initiative for Sharing all Influenza Data) for the B.1.427 and B.1.429 lineages, respectively. This VOC was detected in California and in other US states, and more recently in 34 additional countries worldwide (Fig. 1, A to H, and table S1). The number of B.1.427/B.1.429 genome sequences deposited increased rapidly after December 2020, with an incidence exceeding 50% in California beginning in February 2021 (Fig. 1, B to E). Collectively, this analysis illustrates the increased incidence of the B.1.427/B.1.429 VOC and its progressive geographical spread from California to other US states and other countries, which is consistent with a recent study suggesting enhanced transmissibility relative to the ancestral isolate.

B.1.427/ B.1.429 S reduces sensitivity to vaccine-elicited Abs

To assess the impact of the three mutations present in the B.1.427/B.1.429 S glycoprotein on neutralization, we first compared side by side the neutralization potency of mRNA vaccine–elicited Abs against the G614 S and B.1.427/B.1.429 S pseudoviruses. We used plasma from 15 individuals who received two doses of the Moderna mRNA-1273 vaccine and from 15 individuals who received two doses of Pfizer/BioNtech BNT162b2 vaccine collected between 7 and 27 days after booster immunization (table S2). All vaccinees had substantial plasma-neutralizing activity against G614 SARS-CoV-2 S pseudotyped viruses. Using a murine leukemia virus (MLV) pseudotyping system, geometric mean titers (GMTs) showed that the average neutralization potency of the Moderna mRNA1273–elicited plasma was reduced 2.4-fold for B.1.427/B.1.429 S (GMT: 178) compared with G614 S (GMT: 424) (Fig. 2, A and B; figs. S1 and S2; and table S3), whereas it was reduced 2.3-fold with Pfizer/BioNtech BNT162b2–elicited plasma (B.1.427/B.1.429 GMT: 78 versus G614 GMT: 182) (Fig. 2, C and D; figs. S1 and S2; and table S3). Using a vesicular stomatitis virus (VSV) pseudotyping system, we observed a 2.2-fold average reduction of Moderna mRNA1273–elicited plasma-neutralizing activity against B.1.427/B.1.429 S (GMT: 213) compared with G614 S (GMT: 464) pseudoviruses (Fig. 2, E and F; figs. S1 and S2; and table S3) and a 2.5-fold average reduction of Pfizer/BioNtech BNT162b2–elicited plasma-neutralizing activity against B.1.427/B.1.429 S (GMT: 113) compared with G614 S (GMT: 285) pseudoviruses (Fig. 2, G and H; figs. S1 and S2; and table S3). We also analyzed plasma from 18 individuals, five of whom were previously infected with wild-type (WT) SARS-CoV-2, who received two doses of the Pfizer/BioNtech BNT162b2 vaccine and whose samples were collected between 14 and 28 days after booster immunization. We compared the neutralization potency of Pfizer/BioNtech BNT162b2 vaccine–elicited Abs against D614 S, B.1.427/B.1.429 S, B.1.1.7 S, B.1.351 S, and P.1 S VSV pseudotyped viruses using Vero E6 expressing TMPRSS2 as target cells. GMT plasma neutralization potency was reduced 2.9-fold for B.1.427/B.1.429 S (GMT: 197) compared with D614 S (GMT: 570), which is a decrease comparable to that observed with B.1.351 (GMT: 180, 3.2-fold reduction) and greater than that observed with B.1.1.7 and P.1 (GMT: 450 and 330, 1.3-fold and 1.7-fold reduction, respectively) pseudotyped viruses (Fig. 2, I and J; figs. S1 and S2; and table S3). These data indicate that the three B.1.427/B.1.429 S residue substitutions led to a modest but significant reduction of neutralization potency from vaccine-elicited Abs.

We also analyzed plasma from nine convalescent donors who experienced symptomatic COVID-19 in early 2020 (and consequently were likely exposed to the Wuhan-1 or a closely related SARS-CoV-2 isolate) collected 15 to 28 days after symptom onset (table S2). The neutralization potency of plasma from the nine convalescent donors was reduced 3.4-fold for B.1.427/B.1.429 S (GMT: 70) compared with G614 S (GMT: 240), similar to what we observed with B.1.351 (4.4-fold, GMT: 55) and P.1 (3.3-fold, GMT: 72) pseudotyped viruses, whereas neutralization of B.1.1.7 was less affected (1.9-fold, GMT: 127) (Fig. 2, K and L; figs. S1 and S2; and table S3). In several cases, the level of neutralizing activity against the VOC was found to be below the limit of detection.

These findings show that the three mutations present in the B1.427/B.1.429 S glycoprotein decrease the neutralizing activity of vaccine-elicited and infection-elicited Abs, suggesting that these lineage-defining residue substitutions are associated with immune evasion. However, these data also underscore the higher quality of Ab responses induced by vaccination compared with infection and their enhanced resilience to mutations found in VOC.

B.1.427/B.1.429 S mutations reduce sensitivity to RBD- and NTD-specific Abs

To evaluate the contribution of RBD and NTD substitutions to the reduced neutralization potency of sera from vaccinees and convalescent plasma, we compared the neutralizing activity of 34 RBD and 10 NTD mAbs against the D614 S or B.1.427/B.1.429 S variant using a VSV pseudotyping system.

The panel of RBD-specific mAbs (including six clinical mAbs) recognizes distinct antigenic sites, as previously characterized. Briefly, epitopes span the receptor-binding motif (antigenic sites Ia and Ib), a cryptic antigenic site II, the exposed N343 glycan–containing antigenic site IV, and a second cryptic antigenic site V. A total of 14 out of 34 mAbs showed a reduced neutralization potency when comparing B.1.427/B.1.429 S and D614 S pseudoviruses (Fig. 3, A to C, and fig. S3). Of the six mAbs in clinical use, regdanvimab (CT-P59), and to a smaller extent etesevimab (LY-CoV016), showed a reduction in neutralization potency, whereas bamlanivimab (LY-CoV555) entirely lost its neutralizing activity. Neutralization mediated by the casirivimab/imdevimab mAb cocktail (REGN10933 and REGN10987) and by VIR-7831 (a derivative of S309, recently renamed sotrovimab) was unaffected by the B.1.427/B.1.429 S variant. To address the role of the L452R mutation in the neutralization escape from RBD-specific Abs, we tested the binding of the 34 RBD-specific mAbs to WT and L452R mutant RBD using biolayer interferometry (fig. S4). The 10 RBD-specific mAbs experiencing a 10-fold or greater reduction in neutralization potency of the B.1.427/B.1.429 variant relative to D614 S bound poorly to the L452R RBD mutant, demonstrating a direct role of this mutation in immune evasion.

The neutralizing activity of all 10 NTD-specific mAbs tested was abolished as a result of the presence of the S13I and W152C mutations (Fig. 3, D to F). These data indicate that the decreased potency of neutralization of the B.1.427/B.1.429 variant results from evasion of both RBD- and NTD-specific mAb-mediated neutralization.

Structural characterization of the SARS-CoV-2 B.1.427/B.1.429 S trimer

To visualize the changes in SARS-CoV-2 B.1.427/B.1.429 S that contribute to immune evasion, we determined the cryo–electron microscopy (cryoEM) structure of the variant S ectodomain trimer [carrying the HexaPro mutations] bound to the RBD-specific mAb S2M11 and the NTD-specific mAb S2L20 at 2.3-Å resolution (Fig. 4A, fig. S5, and table S4). S2M11 was used to lock the RBDs in the closed state (Fig. 4B), and S2L20 was used to stabilize the NTDs (Fig. 4C). Superimposing the regdanvimab (CT-P59)–bound and bamlanivimab (LY-CoV555)–bound SARS-CoV-2 RBD structures to B.1.427/B.1.429 S revealed that the introduced L452R is sterically incompatible with binding of these mAbs (Fig. 4, D and E), rationalizing the dampening or loss of neutralizing activity.

We subsequently used local refinement to account for the conformational dynamics of the NTD and S2L20 relative to the rest of S and obtained a cryoEM reconstruction of the NTD bound to S2L20 at 3.0-Å resolution (Fig. 4C, fig. S5, and table S4). The structure revealed that the B.1.427/B.1.429 NTD antigenic supersite is severely altered. The N terminus is disordered up to residue 27, as is the supersite β-hairpin (disordered between residues 137 and 158) and the supersite loop (disordered between residues 243 and 264) (Fig. 4F). These structural changes explain the abrogation of binding and neutralization of the panel of NTD-specific mAbs evaluated.

Overlaying an ACE2-bound SARS-CoV-2 RBD structure with the B.1.427/B.1.429 variant S structure showed that the R452 residue points away from and does not contact ACE2, suggesting that this substitution would not affect receptor engagement (Fig. 4G). We next evaluated binding of the monomeric human ACE2 ectodomain to immobilized B.1.427/B.1.429 and WT RBDs using surface plasmon resonance (fig. S6, A and B, and table S5); biolayer interferometry (fig. S6, C to E, and table S5); and binding of B.1.427/B.1.429, B.1.1.7, and WT RBDs to immobilized human ACE2 by enzyme-linked immunosorbent assay (ELISA) (fig. S6F and table SS5). Our results indicate that the B.1.427/B.1.429 and WT RBDs bound to ACE2 with comparable affinities, whereas the B.1.1.7 RBD had a markedly increased affinity for ACE2, validating the structural observations.

Disulfide bond rearrangement in the B.1.427/B.1.429 variant NTD antigenic supersite

To investigate further the molecular basis for the loss of NTD-directed mAb-neutralizing activity and structural changes in the NTD, we analyzed the binding of a panel of NTD-specific mAbs to recombinant SARS-CoV-2 NTD variants using ELISA. The S13I signal peptide mutation dampened binding of five mAbs and abrogated binding of five additional mAbs of the 11 neutralizing mAbs evaluated (Fig. 5A and fig. S7). Furthermore, the W152C mutation reduced recognition of six NTD-neutralizing mAbs, including a complete loss of binding for two of them, with a pattern complementary to that observed for S13I (Fig. 5A and fig. S7). The B.1.427/B.1.429 S13I/W152C NTD did not bind to any NTD-directed neutralizing mAbs, which are known to target a single antigenic site (antigenic site I), whereas binding of the non-neutralizing S2L20 mAb to the NTD antigenic site IV was not affected by any mutants, confirming proper retention of folding, as supported by the structural data (Fig. 5A and fig. S7). Binding of vaccine-elicited plasma to NTD mutants confirmed and extended these observations with polyclonal Abs by showing an increasingly marked reduction in binding titers caused by the W152C, S13I, and S13I/W152C residue substitutions (Fig. 5B and fig. S8).

We previously showed that disruption of the C15/C136 disulfide bond that connects the N terminus to the rest of the NTD by mutation of either residue or alteration of the signal peptide cleavage site abrogates the neutralizing activity of mAbs targeting the NTD antigenic supersite (site I). Because the S13I substitution resides in the signal peptide and is predicted to shift the signal peptide cleavage site from S13-Q14 to C15-V16, we hypothesized that this substitution indirectly affects the integrity of NTD antigenic site I, which comprises the N terminus. Mass spectrometry analysis of the S13I and S13I/W152C NTD variants confirmed that signal peptide cleavage occurs immediately after residue C15 (Fig. 5, C to E). As a result, C136, which would otherwise be disulfide linked to C15, is cysteinylated in the S13I NTD because of the presence of free cysteine in the expression medium (Fig. 5D and fig. S9). Likewise, the W152C mutation, which introduces a free cysteine, was also found to be cysteinylated in the W152C NTD (Fig. 5F). It is not clear whether cysteinylation would occur during natural infection with S13I or W152C mutants alone or what contribution cysteinylation plays in immune evasion of S13I or W152C mutants alone. Dampening of NTD-specific neutralizing mAb binding is stronger for the S13I mutant than for the S12P mutant, which we previously showed also shifts the signal peptide cleavage site to C15-V16 (Fig. 5A). Conversely, we did not observe any effect on mAb binding of the S12F substitution, which has also been detected in clinical isolates, in agreement with the fact that this mutation did not affect the native signal peptide cleavage site (i.e., it occurs at the S13-Q14 position), as observed by mass spectrometry (Fig. 5G). In the absence of the C15-C136 disulfide bond, the N terminus is no longer stapled to the NTD, consistent with the structural data showing that the N terminus of the B.1.427/B.1.429 variant becomes disordered relative to the rest of the NTD (Fig. 4C).

Although the S13I and W152C NTD variants were respectively cysteinylated at positions C136 and W152C, the double mutant S13I/W152C was not cysteinylated, suggesting that C136 and W152C had formed a new disulfide bond (Fig. 5, D to F). Tandem mass spectrometry analysis of nonreduced, digested peptides identified linked discontinuous peptides containing C136 and W152C (fig. S9), confirming that a disulfide bond forms between C136 and W152C in the S13I/W152C NTD of the B.1.427/B.1.429 variant. W152C is in the β-hairpin of the antigenic supersite, and the formation of a new disulfide bond with C136 would move residues in the β-hairpin >20 Å. The local structure of the β-hairpin was disordered in the B.1.427/B.1.429 variant (Fig. 4C).

Collectively, these findings demonstrate that the S13I and W152C mutations found in the B.1.427/B.1.429 S variant are jointly responsible for escape from NTD-specific mAbs because of deletion of the two SARS-CoV-2 S N-terminal residues and overall rearrangement of the NTD antigenic supersite. Our data support that the SARS-CoV-2 NTD evolved a compensatory mechanism to form an alternative disulfide bond and that mutations of the S signal peptide occur in vivo in a clinical setting to promote immune evasion. The SARS-CoV-2 B.1.427/B.1.429 S variant therefore relies on an indirect and unusual neutralization escape strategy.

Discussion

Serum- or plasma-neutralizing activity is a correlate of protection against SARS-CoV-2 challenge in nonhuman primates, and treatment with several neutralizing mAbs has reduced viral burden and decreased hospitalization and mortality in clinical trials. The observed L452R-mediated immune evasion of B.1.427/B.1.429 S is consistent with previous findings showing that this substitution reduced the binding or neutralizing activity of some mAbs before the discovery of the B.1.427/B.1.429 variant. The acquisition of the L452R substitution by multiple lineages across multiple continents, including the B.1.617.1 and B.1.617.2 lineages emerging in India, is suggestive of positive selection, which might result from the selective pressure of RBD-specific neutralizing Abs.

The SARS-CoV-2 NTD undergoes rapid antigenic drift and accumulates a larger number of mutations and deletions relative to other regions of the S glycoprotein. For instance, the L18F substitution and the deletion of residue Y144 are found in 8% and 26% of viral genomes sequenced and are present in the B.1.351/P.1 lineages and the B.1.1.7 lineage, respectively. Both of these mutations are associated with reduction or abrogation of mAb binding and neutralization. The finding that multiple circulating SARS-CoV-2 variants map to the NTD, several of them in the antigenic supersite (site I), suggests that the NTD is subject to a strong selective pressure from the host humoral immune response. This is further supported by the identification of deletions within the NTD antigenic supersite in immunocompromised hosts with prolonged infections and in the in vitro selection of SARS-CoV-2 S escape variants with NTD mutations that decrease the binding and neutralization potency of COVID-19 convalescent patient sera or mAbs. The data herein showing immune evasion of all tested NTD-specific mAbs by the B.1.427/B.1.429 variant also support that the NTD antigenic supersite is under host immune pressure.

Similar to how the S13I/W152C mutations facilitate evasion of all tested NTD-specific mAbs, E484K causes broad resistance to many RBD-specific mAbs. The independent acquisition of the E484K mutation in the B.1.351, P.1, and B.1.526 variants and, more recently, in the B.1.1.7 variant, suggests this could also occur in the B.1.427/B.1.429 lineages. Indeed, four genome sequences with the E484K RBD mutation in the B.1.427 variant have recently been deposited in GISAID. Alternatively, the S13I/W152C mutations could emerge in any of these variants. The S13I mutation was recently detected in the SARS-CoV-2 B.1.526 lineage, which was originally described in New York. Understanding the newly found mechanism of immune evasion in emerging SARS-CoV-2 variants, such as the signal peptide modification described herein, is as important as sequence surveillance itself to successfully counter the ongoing pandemic.

References 90

  1. 1.

    A. C. Walls, Y. J. Park, M. A. Tortorici, A. Wall, A. T. McGuire, D. Veesler, Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein. Cell 181, 281–292.e6 (2020 ).

    Not in our library10.1016/j.cell.2020.02.058

  2. 2.

    D. Wrapp, N. Wang, K. S. Corbett, J. A. Goldsmith, C. L. Hsieh, O. Abiona, B. S. Graham, J. S. McLellan, Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science 367, 1260–1263 (2020 ).

    Not in our library10.1126/science.abb2507

  3. 3.

    A. C. Walls, M. A. Tortorici, B. J. Bosch, B. Frenz, P. J. M. Rottier, F. DiMaio, F. A. Rey, D. Veesler, Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature 531, 114–117 (2016 ).

    Not in our library10.1038/nature16988

  4. 4.

    M. A. Tortorici, D. Veesler, Structural insights into coronavirus entry. Adv. Virus Res. 105, 93–116 (2019 ).

    Not in our library10.1016/bs.aivir.2019.08.002

  5. 5.

    M. Letko, A. Marzi, V. Munster, Functional assessment of cell entry and receptor usage for SARS-CoV-2 and other lineage B betacoronaviruses. Nat. Microbiol. 5, 562–569 (2020 ).

    Not in our library10.1038/s41564-020-0688-y

  6. 6.

    P. Zhou, X. L. Yang, X. G. Wang, B. Hu, L. Zhang, W. Zhang, H. R. Si, Y. Zhu, B. Li, C. L. Huang, H. D. Chen, J. Chen, Y. Luo, H. Guo, R. D. Jiang, M. Q. Liu, Y. Chen, X. R. Shen, X. Wang, X. S. Zheng, K. Zhao, Q. J. Chen, F. Deng, L. L. Liu, B. Yan, F. X. Zhan, Y. Y. Wang, G. F. Xiao, Z. L. Shi, Addendum: A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature 588, E6 (2020 ).

    Not in our library10.1038/s41586-020-2951-z

  7. 7.

    M. Hoffmann, H. Kleine-Weber, S. Schroeder, N. Krüger, T. Herrler, S. Erichsen, T. S. Schiergens, G. Herrler, N. H. Wu, A. Nitsche, M. A. Müller, C. Drosten, S. Pöhlmann, SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell 181, 271–280.e8 (2020 ).

    Not in our library10.1016/j.cell.2020.02.052

  8. 8.

    W. T. Soh, Y. Liu, E. E. Nakayama, C. Ono, S. Torii, H. Nakagami, Y. Matsuura, T. Shioda, H. Arase, The N-terminal domain of spike glycoprotein mediates SARS-CoV-2 infection by associating with L-SIGN and DC-SIGN. bioRxiv 369264 [Preprint]. 5 November 2020;.

    Not in our library10.1101/2020.11.05.369264

  9. 9.
    AXL is a candidate receptor for SARS-CoV-2 that promotes infection of pulmonary and bronchial epithelial cells · 2021
    No notice
  10. 10.

    D. Pinto, Y. J. Park, M. Beltramello, A. C. Walls, M. A. Tortorici, S. Bianchi, S. Jaconi, K. Culap, F. Zatta, A. De Marco, A. Peter, B. Guarino, R. Spreafico, E. Cameroni, J. B. Case, R. E. Chen, C. Havenar-Daughton, G. Snell, A. Telenti, H. W. Virgin, A. Lanzavecchia, M. S. Diamond, K. Fink, D. Veesler, D. Corti, Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody. Nature 583, 290–295 (2020 ).

    Not in our library10.1038/s41586-020-2349-y

  11. 11.

    L. Piccoli, Y. J. Park, M. A. Tortorici, N. Czudnochowski, A. C. Walls, M. Beltramello, C. Silacci-Fregni, D. Pinto, L. E. Rosen, J. E. Bowen, O. J. Acton, S. Jaconi, B. Guarino, A. Minola, F. Zatta, N. Sprugasci, J. Bassi, A. Peter, A. De Marco, J. C. Nix, F. Mele, S. Jovic, B. F. Rodriguez, S. V. Gupta, F. Jin, G. Piumatti, G. Lo Presti, A. F. Pellanda, M. Biggiogero, M. Tarkowski, M. S. Pizzuto, E. Cameroni, C. Havenar-Daughton, M. Smithey, D. Hong, V. Lepori, E. Albanese, A. Ceschi, E. Bernasconi, L. Elzi, P. Ferrari, C. Garzoni, A. Riva, G. Snell, F. Sallusto, K. Fink, H. W. Virgin, A. Lanzavecchia, D. Corti, D. Veesler, Mapping neutralizing and immunodominant sites on the SARS-CoV-2 spike receptor-binding domain by structure-guided high-resolution serology. Cell 183, 1024–1042.e21 (2020 ).

    Not in our library10.1016/j.cell.2020.09.037

  12. 12.

    M. McCallum, A. De Marco, F. A. Lempp, M. A. Tortorici, D. Pinto, A. C. Walls, M. Beltramello, A. Chen, Z. Liu, F. Zatta, S. Zepeda, J. di Iulio, J. E. Bowen, M. Montiel-Ruiz, J. Zhou, L. E. Rosen, S. Bianchi, B. Guarino, C. S. Fregni, R. Abdelnabi, S. C. Foo, P. W. Rothlauf, L.-M. Bloyet, F. Benigni, E. Cameroni, J. Neyts, A. Riva, G. Snell, A. Telenti, S. P. J. Whelan, H. W. Virgin, D. Corti, M. S. Pizzuto, D. Veesler, N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2. Cell 184, 2332–2347.e16 (2021 ).

    Not in our library10.1016/j.cell.2021.03.028

  13. 13.
    Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms · 2020
    No notice
  14. 14.
    Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail · 2020
    No notice
  15. 15.
    Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies · 2020
    No notice
  16. 16.

    N. Suryadevara, S. Shrihari, P. Gilchuk, L. A. VanBlargan, E. Binshtein, S. J. Zost, R. S. Nargi, R. E. Sutton, E. S. Winkler, E. C. Chen, M. E. Fouch, E. Davidson, B. J. Doranz, R. E. Chen, P.-Y. Shi, R. H. Carnahan, L. B. Thackray, M. S. Diamond, J. E. Crowe Jr., Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. Cell 184, 2316–2331.e15 (2021 ).

    Not in our library10.1016/j.cell.2021.03.029

  17. 17.

    G. Cerutti, Y. Guo, T. Zhou, J. Gorman, M. Lee, M. Rapp, E. R. Reddem, J. Yu, F. Bahna, J. Bimela, Y. Huang, P. S. Katsamba, L. Liu, M. S. Nair, R. Rawi, A. S. Olia, P. Wang, B. Zhang, G.-Y. Chuang, D. D. Ho, Z. Sheng, P. D. Kwong, L. Shapiro, Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite. Cell Host Microbe 29, 819–833.e7 (2021 ).

    Not in our library10.1016/j.chom.2021.03.005

  18. 18.
    A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2 · 2020
    No notice
  19. 19.

    Z. Wang, F. Schmidt, Y. Weisblum, F. Muecksch, C. O. Barnes, S. Finkin, D. Schaefer-Babajew, M. Cipolla, C. Gaebler, J. A. Lieberman, T. Y. Oliveira, Z. Yang, M. E. Abernathy, K. E. Huey-Tubman, A. Hurley, M. Turroja, K. A. West, K. Gordon, K. G. Millard, V. Ramos, J. Da Silva, J. Xu, R. A. Colbert, R. Patel, J. Dizon, C. Unson-O’Brien, I. Shimeliovich, A. Gazumyan, M. Caskey, P. J. Bjorkman, R. Casellas, T. Hatziioannou, P. D. Bieniasz, M. C. Nussenzweig, mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants. Nature 592, 616–622 (2021 ).

    Not in our library10.1038/s41586-021-03324-6

  20. 20.

    C. O. Barnes, C. A. Jette, M. E. Abernathy, K. A. Dam, S. R. Esswein, H. B. Gristick, A. G. Malyutin, N. G. Sharaf, K. E. Huey-Tubman, Y. E. Lee, D. F. Robbiani, M. C. Nussenzweig, A. P. West Jr., P. J. Bjorkman, SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature 588, 682–687 (2020 ).

    Not in our library10.1038/s41586-020-2852-1

  21. 21.

    D. F. Robbiani, C. Gaebler, F. Muecksch, J. C. C. Lorenzi, Z. Wang, A. Cho, M. Agudelo, C. O. Barnes, A. Gazumyan, S. Finkin, T. Hägglöf, T. Y. Oliveira, C. Viant, A. Hurley, H. H. Hoffmann, K. G. Millard, R. G. Kost, M. Cipolla, K. Gordon, F. Bianchini, S. T. Chen, V. Ramos, R. Patel, J. Dizon, I. Shimeliovich, P. Mendoza, H. Hartweger, L. Nogueira, M. Pack, J. Horowitz, F. Schmidt, Y. Weisblum, E. Michailidis, A. W. Ashbrook, E. Waltari, J. E. Pak, K. E. Huey-Tubman, N. Koranda, P. R. Hoffman, A. P. West Jr., C. M. Rice, T. Hatziioannou, P. J. Bjorkman, P. D. Bieniasz, M. Caskey, M. C. Nussenzweig, Convergent antibody responses to SARS-CoV-2 in convalescent individuals. Nature 584, 437–442 (2020 ).

    Not in our library10.1038/s41586-020-2456-9

  22. 22.
    The neutralizing antibody, LY-CoV555, protects against SARS-CoV-2 infection in nonhuman primates · 2021
    No notice
  23. 23.

    A. L. Cathcart, C. Havenar-Daughton, F. A. Lempp, D. Ma, M. Schmid, M. L. Agostini, B. Guarino, J. Diiulio, L. Rosen, H. Tucker, J. Dillen, S. Subramanian, B. Sloan, S. Bianchi, J. Wojcechowskyj, J. Zhou, H. Kaiser, A. Chase, M. Montiel-Ruiz, N. Czudnochowski, E. Cameroni, S. Ledoux, C. Colas, L. Soriaga, A. Telenti, S. Hwang, G. Snell, H. W. Virgin, D. Corti, C. M. Hebner, The dual function monoclonal antibodies VIR-7831 and VIR-7832 demonstrate potent in vitro and in vivo activity against SARS-CoV-2. bioRxiv 434607 [Preprint]. 24 June 2021;.

    Not in our library10.1101/2021.03.09.434607

  24. 24.

    D. Corti, L. A. Purcell, G. Snell, D. Veesler, Tackling COVID-19 with neutralizing monoclonal antibodies. Cell 184, 3086–3108 (2021 ).

    Not in our library10.1016/j.cell.2021.05.005

  25. 25.
    A conserved immunogenic and vulnerable site on the coronavirus spike protein delineated by cross-reactive monoclonal antibodies · 2021
    No notice
  26. 26.
    Cross-reactive serum and memory B-cell responses to spike protein in SARS-CoV-2 and endemic coronavirus infection · 2021
    No notice
  27. 27.

    D. Pinto, M. M. Sauer, N. Czudnochowski, J. S. Low, M. Alejandra Tortorici, M. P. Housley, J. Noack, A. C. Walls, J. E. Bowen, B. Guarino, L. E. Rosen, J. di Iulio, J. Jerak, H. Kaiser, S. Islam, S. Jaconi, N. Sprugasci, K. Culap, R. Abdelnabi, C. S.-Y. Foo, L. Coelmont, I. Bartha, S. Bianchi, C. Silacci-Fregni, J. Bassi, R. Marzi, E. Vetti, A. Cassotta, A. Ceschi, P. Ferrari, P. E. Cippa’, O. Giannini, S. Ceruti, A. Riva, F. Benigni, E. Cameroni, L. Piccoli, M. S. Pizzuto, M. Smithey, D. Hong, A. Telenti, F. A. Lempp, J. Neyts, C. Havenar-Daughton, A. Lanzavecchia, F. Sallusto, G. Snell, H. W. Virgin, M. Beltramello, D. Corti, D. Veesler, A human antibody that broadly neutralizes betacoronaviruses protects against SARS-CoV-2 by blocking the fusion machinery. bioRxiv 442808 [Preprint]. 10 May 2021;.

    Not in our library10.1101/2021.05.09.442808

  28. 28.

    M. M. Sauer, M. A. Tortorici, Y.-J. Park, A. C. Walls, L. Homad, O. J. Acton, J. E. Bowen, C. Wang, X. Xiong, W. de van der Schueren, J. Quispe, B. G. Hoffstrom, B. J. Bosch, A. T. McGuire, D. Veesler, Structural basis for broad coronavirus neutralization. Nat. Struct. Mol. Biol. 28, 478–486 (2021 ).

    Not in our library10.1038/s41594-021-00596-4

  29. 29.

    B. Korber, W. M. Fischer, S. Gnanakaran, H. Yoon, J. Theiler, W. Abfalterer, N. Hengartner, E. E. Giorgi, T. Bhattacharya, B. Foley, K. M. Hastie, M. D. Parker, D. G. Partridge, C. M. Evans, T. M. Freeman, T. I. de Silva, C. McDanal, L. G. Perez, H. Tang, A. Moon-Walker, S. P. Whelan, C. C. LaBranche, E. O. Saphire, D. C. Montefiori, A. Angyal, R. L. Brown, L. Carrilero, L. R. Green, D. C. Groves, K. J. Johnson, A. J. Keeley, B. B. Lindsey, P. J. Parsons, M. Raza, S. Rowland-Jones, N. Smith, R. M. Tucker, D. Wang, M. D. Wyles; Sheffield COVID-19 Genomics Group, Tracking changes in SARS-CoV-2 spike: Evidence that D614G increases infectivity of the COVID-19 virus. Cell 182, 812–827.e19 (2020 ).

    Not in our library10.1016/j.cell.2020.06.043

  30. 30.

    J. A. Plante, Y. Liu, J. Liu, H. Xia, B. A. Johnson, K. G. Lokugamage, X. Zhang, A. E. Muruato, J. Zou, C. R. Fontes-Garfias, D. Mirchandani, D. Scharton, J. P. Bilello, Z. Ku, Z. An, B. Kalveram, A. N. Freiberg, V. D. Menachery, X. Xie, K. S. Plante, S. C. Weaver, P. Y. Shi, Spike mutation D614G alters SARS-CoV-2 fitness. Nature 592, 116–121 (2021 ).

    Not in our library10.1038/s41586-020-2895-3

  31. 31.

    H. Tegally, E. Wilkinson, M. Giovanetti, A. Iranzadeh, V. Fonseca, J. Giandhari, D. Doolabh, S. Pillay, E. J. San, N. Msomi, K. Mlisana, A. von Gottberg, S. Walaza, M. Allam, A. Ismail, T. Mohale, A. J. Glass, S. Engelbrecht, G. Van Zyl, W. Preiser, F. Petruccione, A. Sigal, D. Hardie, G. Marais, M. Hsiao, S. Korsman, M.-A. Davies, L. Tyers, I. Mudau, D. York, C. Maslo, D. Goedhals, S. Abrahams, O. Laguda-Akingba, A. Alisoltani-Dehkordi, A. Godzik, C. K. Wibmer, B. T. Sewell, J. Lourenço, L. C. J. Alcantara, S. L. Kosakovsky Pond, S. Weaver, D. Martin, R. J. Lessells, J. N. Bhiman, C. Williamson, T. de Oliveira, Detection of a SARS-CoV-2 variant of concern in South Africa. Nature 592, 438–443 (2021 ).

    Not in our library10.1038/s41586-021-03402-9

  32. 32.

    N. R. Faria, I. M. Claro, D. Candido, L. A. Moyses Franco, P. S. Andrade, T. M. Coletti, C. A. M. Silva, F. C. Sales, E. R. Manuli, R. S. Aguiar, N. Gaburo, C. da C. Camilo, N. A. Fraiji, M. A. Esashika Crispim, M. do Perpétuo S. S. Carvalho, A. Rambaut, N. Loman, O. G. Pybus, E. C. Sabino, on behalf of CADDE Genomic Network, “Genomic characterisation of an emergent SARS-CoV-2 lineage in Manaus: preliminary findings” (virological.org, 2021); https://virological.org/t/genomic-characterisation-of-an-emergent-sars-cov-2-lineage-in-manaus-preliminary-findings/586.

    Not in our library

  33. 33.
    Estimated transmissibility and impact of SARS-CoV-2 lineage B.1.1.7 in England · 2021
    No notice
  34. 34.
    Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies · 2021
    Corrected
  35. 35.

    P. Wang, M. S. Nair, L. Liu, S. Iketani, Y. Luo, Y. Guo, M. Wang, J. Yu, B. Zhang, P. D. Kwong, B. S. Graham, J. R. Mascola, J. Y. Chang, M. T. Yin, M. Sobieszczyk, C. A. Kyratsous, L. Shapiro, Z. Sheng, Y. Huang, D. D. Ho, Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature 593, 130–135 (2021 ).

    Not in our library10.1038/s41586-021-03398-2

  36. 36.

    S. A. Madhi, V. Baillie, C. L. Cutland, M. Voysey, A. L. Koen, L. Fairlie, S. D. Padayachee, K. Dheda, S. L. Barnabas, Q. E. Bhorat, C. Briner, G. Kwatra, K. Ahmed, P. Aley, S. Bhikha, J. N. Bhiman, A. E. Bhorat, J. du Plessis, A. Esmail, M. Groenewald, E. Horne, S.-H. Hwa, A. Jose, T. Lambe, M. Laubscher, M. Malahleha, M. Masenya, M. Masilela, S. McKenzie, K. Molapo, A. Moultrie, S. Oelofse, F. Patel, S. Pillay, S. Rhead, H. Rodel, L. Rossouw, C. Taoushanis, H. Tegally, A. Thombrayil, S. van Eck, C. K. Wibmer, N. M. Durham, E. J. Kelly, T. L. Villafana, S. Gilbert, A. J. Pollard, T. de Oliveira, P. L. Moore, A. Sigal, A. Izu; NGS-SA Group; Wits-VIDA COVID Group, Efficacy of the ChAdOx1 nCoV-19 Covid-19 vaccine against the B.1.351 variant. N. Engl. J. Med. 384, 1885–1898 (2021 ).

    Not in our library10.1056/nejmoa2102214

  37. 37.

    S. Cele, I. Gazy, L. Jackson, S.-H. Hwa, H. Tegally, G. Lustig, J. Giandhari, S. Pillay, E. Wilkinson, Y. Naidoo, F. Karim, Y. Ganga, K. Khan, M. Bernstein, A. B. Balazs, B. I. Gosnell, W. Hanekom, M. S. Moosa, R. J. Lessells, T. de Oliveira, A. Sigal; Network for Genomic Surveillance in South Africa; COMMIT-KZN Team, Escape of SARS-CoV-2 501Y.V2 from neutralization by convalescent plasma. Nature 593, 142–146 (2021 ).

    Not in our library10.1038/s41586-021-03471-w

  38. 38.

    D. Planas, T. Bruel, L. Grzelak, F. Guivel-Benhassine, I. Staropoli, F. Porrot, C. Planchais, J. Buchrieser, M. M. Rajah, E. Bishop, M. Albert, F. Donati, M. Prot, S. Behillil, V. Enouf, M. Maquart, M. Smati-Lafarge, E. Varon, F. Schortgen, L. Yahyaoui, M. Gonzalez, J. De Sèze, H. Péré, D. Veyer, A. Sève, E. Simon-Lorière, S. Fafi-Kremer, K. Stefic, H. Mouquet, L. Hocqueloux, S. van der Werf, T. Prazuck, O. Schwartz, Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies. Nat. Med. 27, 917–924 (2021 ).

    Not in our library10.1038/s41591-021-01318-5

  39. 39.

    C. K. Wibmer, F. Ayres, T. Hermanus, M. Madzivhandila, P. Kgagudi, B. Oosthuysen, B. E. Lambson, T. de Oliveira, M. Vermeulen, K. van der Berg, T. Rossouw, M. Boswell, V. Ueckermann, S. Meiring, A. von Gottberg, C. Cohen, L. Morris, J. N. Bhiman, P. L. Moore, SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma. Nat. Med. 27, 622–625 (2021 ).

    Not in our library10.1038/s41591-021-01285-x

  40. 40.

    X. Xie, Y. Liu, J. Liu, X. Zhang, J. Zou, C. R. Fontes-Garfias, H. Xia, K. A. Swanson, M. Cutler, D. Cooper, V. D. Menachery, S. C. Weaver, P. R. Dormitzer, P.-Y. Shi, Neutralization of SARS-CoV-2 spike 69/70 deletion, E484K and N501Y variants by BNT162b2 vaccine-elicited sera. Nat. Med. 27, 620–621 (2021 ).

    Not in our library10.1038/s41591-021-01270-4

  41. 41.

    A. Rambaut, E. C. Holmes, Á. O’Toole, V. Hill, J. T. McCrone, C. Ruis, L. du Plessis, O. G. Pybus, A dynamic nomenclature proposal for SARS-CoV-2 lineages to assist genomic epidemiology. Nat. Microbiol. 5, 1403–1407 (2020 ).

    Not in our library10.1038/s41564-020-0770-5

  42. 42.

    X. Deng, M. A. Garcia-Knight, M. M. Khalid, V. Servellita, C. Wang, M. K. Morris, A. Sotomayor-González, D. R. Glasner, K. R. Reyes, A. S. Gliwa, N. P. Reddy, C. Sanchez San Martin, S. Federman, J. Cheng, J. Balcerek, J. Taylor, J. A. Streithorst, S. Miller, B. Sreekumar, P.-Y. Chen, U. Schulze-Gahmen, T. Y. Taha, J. M. Hayashi, C. R. Simoneau, G. R. Kumar, S. McMahon, P. V. Lidsky, Y. Xiao, P. Hemarajata, N. M. Green, A. Espinosa, C. Kath, M. Haw, J. Bell, J. K. Hacker, C. Hanson, D. A. Wadford, C. Anaya, D. Ferguson, P. A. Frankino, H. Shivram, L. F. Lareau, S. K. Wyman, M. Ott, R. Andino, C. Y. Chiu, Transmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant. Cell 184, 3426–3437.e8 (2021 ).

    Not in our library10.1016/j.cell.2021.04.025

  43. 43.

    J. K. Millet, G. R. Whittaker, Murine leukemia virus (MLV)-based coronavirus spike-pseudotyped particle production and infection. Bio Protoc. 6, e2035 (2016 ).

    Not in our library10.21769/bioprotoc.2035

  44. 44.

    T. N. Starr, N. Czudnochowski, F. Zatta, Y.-J. Park, Z. Liu, A. Addetia, D. Pinto, M. Beltramello, P. Hernandez, A. J. Greaney, R. Marzi, W. G. Glass, I. Zhang, A. S. Dingens, J. E. Bowen, J. A. Wojcechowskyj, A. De Marco, L. E. Rosen, J. Zhou, M. Montiel-Ruiz, H. Kaiser, H. Tucker, M. P. Housley, J. di Iulio, G. Lombardo, M. Agostini, N. Sprugasci, K. Culap, S. Jaconi, M. Meury, E. Dellota, E. Cameroni, T. I. Croll, J. C. Nix, C. Havenar-Daughton, A. Telenti, F. A. Lempp, M. S. Pizzuto, J. D. Chodera, C. M. Hebner, S. P. J. Whelan, H. W. Virgin, D. Veesler, D. Corti, J. D. Bloom, G. Snell, Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape. bioRxiv 438709 [Preprint]. 8 April 2021.

    Not in our library10.1101/2021.04.06.438709

  45. 45.

    M. A. Tortorici, N. Czudnochowski, T. N. Starr, R. Marzi, A. C. Walls, F. Zatta, J. E. Bowen, S. Jaconi, J. di Iulio, Z. Wang, A. De Marco, S. K. Zepeda, D. Pinto, Z. Liu, M. Beltramello, I. Bartha, M. P. Housley, F. A. Lempp, L. E. Rosen, E. Dellota, H. Kaiser, M. Montiel-Ruiz, J. Zhou, A. Addetia, B. Guarino, K. Culap, N. Sprugasci, C. Saliba, E. Vetti, I. Giacchetto-Sasselli, C. S. Fregni, R. Abdelnabi, S.-Y. C. Foo, C. Havenar-Daughton, M. A. Schmid, F. Benigni, E. Cameroni, J. Neyts, A. Telenti, G. Snell, H. W. Virgin, S. P. J. Whelan, J. D. Bloom, D. Corti, D. Veesler, M. S. Pizzuto, Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody. bioRxiv 438818 [Preprint]. 8 April 2021;.

    Not in our library10.1101/2021.04.07.438818

  46. 46.
    Structure-based design of prefusion-stabilized SARS-CoV-2 spikes · 2020
    No notice
  47. 47.

    K. McMahan, J. Yu, N. B. Mercado, C. Loos, L. H. Tostanoski, A. Chandrashekar, J. Liu, L. Peter, C. Atyeo, A. Zhu, E. A. Bondzie, G. Dagotto, M. S. Gebre, C. Jacob-Dolan, Z. Li, F. Nampanya, S. Patel, L. Pessaint, A. Van Ry, K. Blade, J. Yalley-Ogunro, M. Cabus, R. Brown, A. Cook, E. Teow, H. Andersen, M. G. Lewis, D. A. Lauffenburger, G. Alter, D. H. Barouch, Correlates of protection against SARS-CoV-2 in rhesus macaques. Nature 590, 630–634 (2021 ).

    Not in our library10.1038/s41586-020-03041-6

  48. 48.

    P. S. Arunachalam, A. C. Walls, N. Golden, C. Atyeo, S. Fischinger, C. Li, P. Aye, M. J. Navarro, L. Lai, V. V. Edara, K. Röltgen, K. Rogers, L. Shirreff, D. E. Ferrell, S. Wrenn, D. Pettie, J. C. Kraft, M. C. Miranda, E. Kepl, C. Sydeman, N. Brunette, M. Murphy, B. Fiala, L. Carter, A. G. White, M. Trisal, C.-L. Hsieh, K. Russell-Lodrigue, C. Monjure, J. Dufour, S. Spencer, L. Doyle-Meyers, R. P. Bohm, N. J. Maness, C. Roy, J. A. Plante, K. S. Plante, A. Zhu, M. J. Gorman, S. Shin, X. Shen, J. Fontenot, S. Gupta, D. T. O’Hagan, R. Van Der Most, R. Rappuoli, R. L. Coffman, D. Novack, J. S. McLellan, S. Subramaniam, D. Montefiori, S. D. Boyd, J. A. L. Flynn, G. Alter, F. Villinger, H. Kleanthous, J. Rappaport, M. S. Suthar, N. P. King, D. Veesler, B. Pulendran, Adjuvanting a subunit COVID-19 vaccine to induce protective immunity. Nature 594, 253–258 (2021 ).

    Not in our library10.1038/s41586-021-03530-2

  49. 49.
    REGN-COV2 antibodies prevent and treat SARS-CoV-2 infection in rhesus macaques and hamsters · 2020
    No notice
  50. 50.

    Z. Liu, L. A. VanBlargan, L.-M. Bloyet, P. W. Rothlauf, R. E. Chen, S. Stumpf, H. Zhao, J. M. Errico, E. S. Theel, M. J. Liebeskind, B. Alford, W. J. Buchser, A. H. Ellebedy, D. H. Fremont, M. S. Diamond, S. P. J. Whelan, Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization. Cell Host Microbe 29, 477–488.e4 (2021 ).

    Not in our library10.1016/j.chom.2021.01.014

  51. 51.

    Q. Li, J. Wu, J. Nie, L. Zhang, H. Hao, S. Liu, C. Zhao, Q. Zhang, H. Liu, L. Nie, H. Qin, M. Wang, Q. Lu, X. Li, Q. Sun, J. Liu, L. Zhang, X. Li, W. Huang, Y. Wang, The impact of mutations in SARS-CoV-2 spike on viral infectivity and antigenicity. Cell 182, 1284–1294.e9 (2020 ).

    Not in our library10.1016/j.cell.2020.07.012

  52. 52.
    Complete map of SARS-CoV-2 RBD mutations that escape the monoclonal antibody LY-CoV555 and its cocktail with LY-CoV016 · 2021
    No notice
  53. 53.
    Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding · 2020
    No notice
  54. 54.

    V.-V. Edara, L. Lai, M. K. Sahoo, K. Floyd, M. Sibai, D. Solis, M. W. Flowers, L. Hussaini, C. R. Ciric, S. Bechnack, K. Stephens, E. B. Mokhtari, P. Mudvari, A. Creanga, A. Pegu, A. Derrien-Colemyn, A. R. Henry, M. Gagne, B. S. Graham, J. Wrammert, D. C. Douek, E. Boritz, B. A. Pinsky, M. S. Suthar, Infection and vaccine-induced neutralizing antibody responses to the SARS-CoV-2 B.1.617.1 variant. bioRxiv 443299 [Preprint]. 10 May 2021;.

    Not in our library10.1101/2021.05.09.443299

  55. 55.
    Acquisition of the L452R Mutation in the ACE2-Binding Interface of Spike Protein Triggers Recent Massive Expansion of SARS-CoV-2 Variants · 2021
    No notice
  56. 56.
    Circulating SARS-CoV-2 spike N439K variants maintain fitness while evading antibody-mediated immunity · 2021
    No notice
  57. 57.

    V. A. Avanzato, M. J. Matson, S. N. Seifert, R. Pryce, B. N. Williamson, S. L. Anzick, K. Barbian, S. D. Judson, E. R. Fischer, C. Martens, T. A. Bowden, E. de Wit, F. X. Riedo, V. J. Munster, Case study: Prolonged infectious SARS-CoV-2 shedding from an asymptomatic immunocompromised individual with cancer. Cell 183, 1901–1912.e9 (2020 ).

    Not in our library10.1016/j.cell.2020.10.049

  58. 58.

    B. Choi, M. C. Choudhary, J. Regan, J. A. Sparks, R. F. Padera, X. Qiu, I. H. Solomon, H. H. Kuo, J. Boucau, K. Bowman, U. D. Adhikari, M. L. Winkler, A. A. Mueller, T. Y. Hsu, M. Desjardins, L. R. Baden, B. T. Chan, B. D. Walker, M. Lichterfeld, M. Brigl, D. S. Kwon, S. Kanjilal, E. T. Richardson, A. H. Jonsson, G. Alter, A. K. Barczak, W. P. Hanage, X. G. Yu, G. D. Gaiha, M. S. Seaman, M. Cernadas, J. Z. Li, Persistence and evolution of SARS-CoV-2 in an immunocompromised host. N. Engl. J. Med. 383, 2291–2293 (2020 ).

    Not in our library10.1056/nejmc2031364

  59. 59.
    Recurrent deletions in the SARS-CoV-2 spike glycoprotein drive antibody escape · 2021
    No notice
  60. 60.
    SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma · 2021
    No notice
  61. 61.
    SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma · 2021
    No notice
  62. 62.
    Emergence and expansion of SARS-CoV-2 B.1.526 after identification in New York · 2021
    No notice
  63. 63.

    A. P. West Jr., C. O. Barnes, Z. Yang, P. J. Bjorkman, SARS-CoV-2 lineage B.1.526 emerging in the New York region detected by software utility created to query the spike mutational landscape. bioRxiv 431043 [Preprint]. 22 April 2021;.

    Not in our library10.1101/2021.02.14.431043

  64. 64.
    Automated generation of heuristics for biological sequence comparison · 2005
    No notice
  65. 65.

    K. Katoh, D. M. Standley, MAFFT multiple sequence alignment software version 7: Improvements in performance and usability. Mol. Biol. Evol. 30, 772–780 (2013 ).

    Not in our library10.1093/molbev/mst010

  66. 66.

    D. Corti, J. Voss, S. J. Gamblin, G. Codoni, A. Macagno, D. Jarrossay, S. G. Vachieri, D. Pinna, A. Minola, F. Vanzetta, C. Silacci, B. M. Fernandez-Rodriguez, G. Agatic, S. Bianchi, I. Giacchetto-Sasselli, L. Calder, F. Sallusto, P. Collins, L. F. Haire, N. Temperton, J. P. Langedijk, J. J. Skehel, A. Lanzavecchia, A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850–856 (2011 ).

    Not in our library10.1126/science.1205669

  67. 67.

    J. Gregson, S. Y. Rhee, R. Datir, D. Pillay, C. F. Perno, A. Derache, R. S. Shafer, R. K. Gupta, Human immunodeficiency virus-1 viral load is elevated in individuals with reverse-transcriptase mutation M184V/I during virological failure of first-line antiretroviral therapy and is associated with compensatory mutation L74I. J. Infect. Dis. 222, 1108–1116 (2020 ).

    Not in our library10.1093/infdis/jiz631

  68. 68.
    Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV · 2020
    Corrected
  69. 69.

    A. Takada, C. Robison, H. Goto, A. Sanchez, K. G. Murti, M. A. Whitt, Y. Kawaoka, A system for functional analysis of Ebola virus glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 94, 14764–14769 (1997 ).

    Not in our library10.1073/pnas.94.26.14764

  70. 70.

    A. M. Riblett, V. A. Blomen, L. T. Jae, L. A. Altamura, R. W. Doms, T. R. Brummelkamp, J. A. Wojcechowskyj, A haploid genetic screen identifies heparan sulfate proteoglycans supporting Rift Valley fever virus infection. J. Virol. 90, 1414–1423 (2015 ).

    Not in our library10.1128/jvi.02055-15

  71. 71.
    Protocol and Reagents for Pseudotyping Lentiviral Particles with SARS-CoV-2 Spike Protein for Neutralization Assays · 2020
    No notice
  72. 72.
    Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2 · 2020
    No notice
  73. 73.

    J. B. Case, P. W. Rothlauf, R. E. Chen, N. M. Kafai, J. M. Fox, B. K. Smith, S. Shrihari, B. T. McCune, I. B. Harvey, S. P. Keeler, L. M. Bloyet, H. Zhao, M. Ma, L. J. Adams, E. S. Winkler, M. J. Holtzman, D. H. Fremont, S. P. J. Whelan, M. S. Diamond, Replication-competent vesicular stomatitis virus vaccine vector protects against SARS-CoV-2-mediated pathogenesis in mice. Cell Host Microbe 28, 465–474.e4 (2020 ).

    Not in our library10.1016/j.chom.2020.07.018

  74. 74.

    C. Suloway, J. Pulokas, D. Fellmann, A. Cheng, F. Guerra, J. Quispe, S. Stagg, C. S. Potter, B. Carragher, Automated molecular microscopy: The new Leginon system. J. Struct. Biol. 151, 41–60 (2005 ).

    Not in our library10.1016/j.jsb.2005.03.010

  75. 75.

    D. Tegunov, P. Cramer, Real-time cryo-electron microscopy data preprocessing with Warp. Nat. Methods 16, 1146–1152 (2019 ).

    Not in our library10.1038/s41592-019-0580-y

  76. 76.

    A. Punjani, H. Zhang, D. J. Fleet, Non-uniform refinement: Adaptive regularization improves single-particle cryo-EM reconstruction. Nat. Methods 17, 1214–1221 (2020 ).

    Not in our library10.1038/s41592-020-00990-8

  77. 77.
    New tools for automated high-resolution cryo-EM structure determination in RELION-3 · 2018
    No notice
  78. 78.
    A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis · 2019
    No notice
  79. 79.
    High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy · 2013
    No notice
  80. 80.

    E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt, E. C. Meng, T. E. Ferrin, UCSF Chimera—A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004 ).

    Not in our library10.1002/jcc.20084

  81. 81.
    Features and development of Coot · 2010
    No notice
  82. 82.
    Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta · 2016
    No notice
  83. 83.

    B. Frenz, S. Rämisch, A. J. Borst, A. C. Walls, J. Adolf-Bryfogle, W. R. Schief, D. Veesler, F. DiMaio, Automatically Fixing Errors in Glycoprotein Structures with Rosetta. Structure 27, 134–139.e3 (2019 ).

    Not in our library10.1016/j.str.2018.09.006

  84. 84.

    F. DiMaio, Y. Song, X. Li, M. J. Brunner, C. Xu, V. Conticello, E. Egelman, T. Marlovits, Y. Cheng, D. Baker, Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement. Nat. Methods 12, 361–365 (2015 ).

    Not in our library10.1038/nmeth.3286

  85. 85.
    Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix · 2019
    No notice
  86. 86.
    ISOLDE : a physically realistic environment for model building into low-resolution electron-density maps · 2018
    No notice
  87. 87.
    MolProbity : all-atom structure validation for macromolecular crystallography · 2009
    No notice
  88. 88.

    B. A. Barad, N. Echols, R. Y. Wang, Y. Cheng, F. DiMaio, P. D. Adams, J. S. Fraser, EMRinger: Side chain-directed model and map validation for 3D cryo-electron microscopy. Nat. Methods 12, 943–946 (2015 ).

    Not in our library10.1038/nmeth.3541

  89. 89.

    J. Agirre, J. Iglesias-Fernández, C. Rovira, G. J. Davies, K. S. Wilson, K. D. Cowtan, Privateer: Software for the conformational validation of carbohydrate structures. Nat. Struct. Mol. Biol. 22, 833–834 (2015 ).

    Not in our library10.1038/nsmb.3115

  90. 90.

    T. D. Goddard, C. C. Huang, E. C. Meng, E. F. Pettersen, G. S. Couch, J. H. Morris, T. E. Ferrin, UCSF ChimeraX: Meeting modern challenges in visualization and analysis. Protein Sci. 27, 14–25 (2018 ).

    Not in our library10.1002/pro.3235

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