Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera
Open accessAbstract
SARS-CoV-2 has caused over 2 million deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9 amino acid changes in the spike, including N501Y in the ACE2 interacting surface. We examine the ability of B.1.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by structure/function analysis of a large panel of well-characterized monoclonal antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light-chain contacts with residue 501. However, widespread escape from monoclonal antibodies or antibody responses generated by natural infection or vaccination was not observed.
Verified 2026-10-06 · 2 references not checked yet
AI snapshot
Written from the paper’s full text.
TL;DR
The SARS-CoV-2 B.1.1.7 variant is harder to neutralize than the early Victoria strain by convalescent and vaccine sera, with reduced potency partly attributable to the N501Y spike mutation. However, the paper finds no widespread escape from monoclonal antibodies or from natural infection- or vaccine-induced antibody responses.
Key findings
- B.1.1.7 required higher serum concentrations for neutralization: convalescent plasma FRNT50 titers were 2.9-fold lower against B.1.1.7 than Victoria (geometric mean, n = 34, p < 0.0001); AstraZeneca AZD1222 vaccine sera showed 2.5-fold (n = 15, p < 0.0001) and 2.1-fold (n = 10, p < 0.002) reductions at 14 and 28 days after the second dose; Pfizer-BioNTech BNT162b2 sera showed a 3.3-fold reduction (n = 25, p < 0.0001).
- N501Y increased RBD binding affinity for ACE2 approximately 7-fold by biolayer interferometry: WT RBD(501N)-ACE2 KD 75.1 nM versus RBD(501Y)-ACE2 KD 10.7 nM, due to a slower off rate.
- Some public IGHV3-53 antibodies were affected: mAbs 150, 158, and 175 showed roughly 3-fold reduced affinity, mAb 269 was hypersensitive with a 30-fold affinity effect and almost complete loss of neutralization, and mAb 278 failed to reach 100% neutralization with a maximum of 78%. Regeneron and AstraZeneca antibodies showed only modest or no reduction.
- Plasma from 13 patients infected with B.1.1.7 showed no significant difference in neutralization titers between B.1.1.7 and Victoria strains.
Methods
- The study analyzed 377 spike-targeting mAbs from first-wave SARS-CoV-2 cases, focusing on 20 potent neutralizing antibodies (19 anti-RBD, 1 anti-NTD), using BLI binding assays, crystallography of Fab 269 with WT and N501Y RBD, and focus reduction neutralization tests (FRNT) against Victoria and B.1.1.7.
- Neutralization was tested with 34 convalescent plasma samples, AstraZeneca AZD1222 vaccine sera at 14 days (n = 15) and 28 days (n = 10) after the second dose, Pfizer-BioNTech BNT162b2 vaccine sera (n = 25) 7–17 days after the second dose, and plasma from 13 B.1.1.7-infected patients.
- COG-UK sequence analysis examined 180,000 sequences; statistical comparisons used the Wilcoxon matched-pairs signed-rank test with two-tailed p values and geometric means.
Limitations
- Stated: correlates of protection from SARS-CoV-2 are not established; in vitro neutralization assays do not capture contributions from T cells, Fcγ receptor interactions, or complement activation; convalescent plasma and vaccine serum were taken relatively soon after infection or vaccination, so titers may drop over time.
- Stated: further work is needed to understand antibody responses to B.1.1.7, including adaptation to N501Y and NTD deletions, and to test neutralization of other variants such as B.1.351 and P.1.
- Evident from the text: some groups were small (e.g., n = 10, n = 13, n = 15, n = 25), and the study reports in vitro neutralization only, without in vivo protection or durability data.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
0 of 10 cited sources checked · 0 supported · 0 flagged
- Findingown data
BLI comparing binding of potently neutralizing mAbs to 501Y and 501N RBDs showed little effect on many potent antibodies, for instance IGVH1-58 antibodies 55, 165, 253, and 318.
“As expected, there is little effect on many potent antibodies, for instance, the IGVH1-58 antibodies: 55, 165, 253, and 318.”
Quote in the paperNot a substantial claim - Findingown data
The common IGLV1-9 antibodies mAbs 150 and 158 show a consistent reduction in affinity of roughly 3-fold.
“the common IGLV1-9 antibodies (mAbs 150 and 158) show a consistent reduction in affinity of roughly 3-fold (Figure 3A).”
Quote in the paperNot a substantial claim - Findingown data
mAb 222, which pairs IGHV3-53 with IGLV3-20, shows no reduction in binding to 501Y RBD.
“In contrast, mAb 222, which pairs IGHV3-53 with IGLV3-20, shows no reduction.”
Quote in the paperNot a substantial claim - Findingown data
Potent mAbs mapped to positions overlapping or closely adjacent to the ACE2 binding surface at the apex of the RBD and tended to have few somatic mutations (on average 5.33 heavy-chain and 4.33 light-chain amino acids).
“Potent mAbs mapped to positions either overlapping or closely adjacent to the ACE2 binding surface at the apex of the RBD (Figures 1B and 1C) and tended to have rather few somatic mutations (on average 5.33 and 4.33 amino acids in the heavy and light chains [HC, LC], respectively).”
Quote in the paperNot a substantial claim - Findingown data
For the Pfizer-BioNTech BNT162b2 vaccine, the reduction in neutralization titers between B.1.1.7 and Victoria was 3.3-fold (n = 25, p < 0.0001).
“For the Pfizer-BioNTech vaccine BNT162b2, the reduction was 3.3-fold (geometric mean, n = 25 p < 0.0001) (Figure 5C).”
Quote in the paperSubstantial claim
- Findingown data
Mass spectrometry and biolayer interferometry data confirmed the presence of tyrosine at position 501.
“Mass spectrometry and biolayer interferometry data confirmed the presence of tyrosine at 501.”
Quote in the paperNot a substantial claim - Findingown data
There is a marked approximately 3-fold effect for mAb 40 (IGHV3-66) and for most of the important IGHV3-53 antibodies (150, 158, and 175).
“There is a marked ∼3-fold effect for mAb 40 (IGHV3-66) and for most of the important IGHV3-53 antibodies (150, 158, and 175).”
Quote in the paperSubstantial claim - Findingown data
A mixture of all three N501Y subgroups at the outset in late October resolved into dominance of the B.1.1.7 variant over about 2 months.
“A mixture of all three subgroups at the outset in late October resolved into the dominance of the B.1.1.7 variant over the course of about 2 months (Figure S1A)”
Quote in the paperNot a substantial claim - Findingown data
Only a modest effect was observed for the late-stage clinical trial mAbs Regeneron REGN10933 and REGN10987 and AstraZeneca AZD1061 and AZD8895.
“Only a modest effect was observed with these antibodies (Figure 2C).”
Quote in the paperNot a substantial claim - Findingown data
Analysis of 180,000 COG-UK sequences showed one major and two minor subgroups of the approximately 13,700 identifiable N501Y-harboring variants.
“Analysis of 180,000 sequences from the COG-UK database (https://www.cogconsortium.uk) showed one major and two minor subgroups (Figure S1A) of the ∼13,700 identifiable variants harboring N501Y distinguishable by cluster analysis (STAR Methods).”
Quote in the paperNot a substantial claim - Findingown data
mAb 269, a VH3-53 mAb paired with the IGLV1-9 light chain, appears hyper-sensitive to N501Y, with a 30-fold effect.
“mAb 269, which is also a VH3-53 mAb, paired with the IGLV1-9 light chain, however, appears hyper-sensitive to the mutation (30-fold effect).”
Quote in the paperNot a substantial claim - Findingown data
Neutralization by the AstraZeneca antibodies AZD1061 and AZD8895 was little affected by B.1.1.7.
“The neutralization of the AZ antibodies AZD1061 and AZD8895 was similarly little affected.”
Quote in the paperNot a substantial claim - Findingown data
Among 34 convalescent samples including the WHONIBSC 20/130 reference serum, FRNT50 dilutions for B.1.1.7 were 2.9-fold lower (geometric mean) than for Victoria (p < 0.0001).
“We analyzed 34 convalescent samples including the WHONIBSC 20/130 reference serum, and, although a few sera showed near identical FRNT 50 values, the FRNT50 dilutions for the B.1.1.7 strain were 2.9-fold lower (geometric mean) than those for the Victoria strain (p < 0.0001).”
Quote in the paperSubstantial claim - Findingown data
AstraZeneca AZD1222 vaccine sera showed a 2.5-fold (n = 15, p < 0.0001) and 2.1-fold (n = 10, p < 0.002) reduction in neutralization titers between B.1.1.7 and Victoria at 14 and 28 days after the second dose, respectively.
“Neutralization assays against B.1.1.7 and Victoria strains showed a 2.5-fold (geometric mean n = 15, p < 0.0001) and 2.1-fold (geometric mean, n = 10, p < 0.002) reduction in the neutralization titers between B.1.1.7 and Victoria strains for the AstraZeneca vaccine after 14 and 28 days following the second dose, respectively (Figure 5B).”
Quote in the paperSubstantial claim - Findingown data
The crystal structure of Fab 269 in complex with WT RBD at 1.8 Å resolution shows similar interactions to those observed for mAbs 150 and 158.
“The structure of Fab 269 in complex with WT RBD determined at 1.8 Å resolution (STAR Methods; Table S1; Figure 3C) shows similar interactions to those observed for mAbs 150 and 158.”
Quote in the paperNot a substantial claim - Findingown data
For 13 patients infected with B.1.1.7, there was no significant difference between neutralization titers for B.1.1.7 and Victoria.
“For these samples as a whole, there was no significant difference between the neutralization titers for the two viruses (Figure 6B)”
Quote in the paperSubstantial claim - Findingown data
For antibodies 40, 88, 222, 316, 384, and 398, FRNT50 values between B.1.1.7 and Victoria strains were minimally affected (<2-fold difference).
“For some antibodies (40, 88, 222, 316, 384, 398), FRNT 50 values between B.1.1.7 and Victoria strains were minimally affected (<2-fold difference).”
Quote in the paperNot a substantial claim - Premisecitation
B.1.1.7 contains a total of 9 changes in the spike protein relative to Wuhan: N501Y, A570D, D614G, P681H, T716I, S982A, D1119H, and deletions of residues 69-70 and 144.
“B.1.1.7 contains a total of 9 changes in the spike protein relative to Wuhan: N501Y, A570D, D614G, P681H, T716I, S982A, D1119H, and deletions of residues 69–70 and 144.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Rambaut et al., 2020
Not checked in the free run.
- Premisecitation
In the prior study, all 20 potent neutralizing antibodies (FRNT50 <0.1 μg/mL for Victoria) bound the RBD, except mAb 159, which bound the NTD.
“In that study, neutralization titers established that all 20 potent neutralizing antibodies (FRNT50 <0.1 μg/mL for the Victoria virus) bound the RBD, with the single exception of mAb 159, which bound the NTD.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Dejnirattisai et al., 2021 source
Not checked in the free run.
- Interpretationown data
There is a modest reduction in neutralization titers against B.1.1.7 by convalescent and vaccine sera generated to early strains of SARS-CoV-2.
“In summary, we describe here a modest reduction in the neutralization titers against B.1.1.7 by convalescent and vaccine sera generated to early strains of SARS-CoV-2 and give a structural/biophysical description of how this may be driven.”
Quote in the paperSubstantial claim - Interpretationown data
Infection with B.1.1.7 will afford protection from infection with earlier variants.
“meaning that infection with B.1.1.7 will afford protection from infection with earlier variants.”
Quote in the paperSubstantial claim - Interpretationreasoning
In the context of a multivalent interaction at the cell surface, the effect of N501Y on ACE2 affinity would be amplified.
“In the context of a multivalent interaction at the cell surface, this effect would be amplified.”
Quote in the paperSubstantial claim - Interpretationown data
The Δ69-70 mutation may be driving the evolutionary advantage of B.1.1.7 over the two other N501Y-containing forms.
“suggesting the Δ69-70 mutation may be driving the evolutionary advantage over these two other forms.”
Quote in the paperNot a substantial claim - Interpretationreasoning
The majority of IGHV3-53 and IGHV3-66 antibodies would be expected to be affected by N501Y because their interaction with asparagine is strongly favorable.
“We would expect the majority of these antibodies to be affected by the mutation, since, for them, unlike ACE2, the interaction with the asparagine is strongly favorable (Figure 2B).”
Quote in the paperSubstantial claim - Interpretationown data
Analysis of the N501Y position suggests that binding of over half of the structurally characterized potent mAbs would be unaffected by the change.
“Analysis of the position of the N501Y change with respect to the binding of all structurally characterized potent mAbs suggests that the binding of over half of the antibodies would be unaffected by the change (Figure 2A).”
Quote in the paperNot a substantial claim - Interpretationown data
The increased ACE2 affinity is in line with enhanced interactions of the tyrosine side chain with residues Y41 and K353 of ACE2.
“This is in-line with enhanced interactions of the tyrosine side chain with the side chains of residues Y41 and K353 of ACE2 (Figure 1D).”
Quote in the paperNot a substantial claim - Interpretationreasoning
The increase in transmission of B.1.1.7 is compounded by the reduction in neutralization potency of antibodies generated by prior infection.
“Here, we show that this increase in transmission is compounded by the reduction in neutralization potency of antibodies generated by prior infection.”
Quote in the paperSubstantial claim - Interpretationown data
For IGHV3-53 and IGHV3-66 antibodies, the mode of binding is dictated by HC CDR1 and CDR2, orienting the light-chain CDR1 region atop residue 501.
“For these and the IGHV3-66 antibodies, the mode of binding is dictated by the HC CDR1 and CDR2, which orientates the antibody such that the light-chain CDR1 region lies atop residue 501.”
Quote in the paperSubstantial claim - Interpretationnone given
B.1.1.7 contains additional mutations that may affect neutralization, in particular the deletions at 69-70 and 144 in the NTD.
“However, B.1.1.7 contains additional mutations that may have a bearing on neutralization, in particular, the deletions at 69–70 and 144 in the NTD.”
Quote in the paperNot a substantial claim
- Classified as probably not a substantial claim. 24
- May combine two claims. 24
Probably not a substantial claim: may not pass S3 (load-bearing).
Findingown dataElectron density for the side chain of Y501 is weak.
“Electron density for the side chain of Y501 is weak.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataFor the Regeneron antibodies, neutralization of REGN10987 was unaffected by B.1.1.7, while REGN10933 showed a slight reduction but retained potent activity.
“For the Regeneron antibodies, the neutralization of REGN10987 was unaffected by B.1.1.7, while REGN10933 showed a slight reduction but still retained potent activity (Figure 4B; Table S2).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Findingown dataThe structures of N501Y RBD/269 Fab and RBD/269 Fab complexes were determined with Rwork/Rfree = 0.197/0.222 and 0.185/0.200, respectively.
“resulted in the current structures with Rwork/ Rfree = 0.197/ 0.222 and Rwork/ Rfree = 0.185/0.200 for all data to 2.19 Å and 1.77 Å resolution for N501Y RBD/269 Fab and RBD/269 Fab complexes, respectively.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataFor other antibodies, there was a fall in neutralization titers for B.1.1.7, particularly mAb 269, where neutralization was almost completely lost, and mAb 278, which failed to reach 100% neutralization with a maximum of only 78%.
“However, for others there was a fall in the neutralization titers for B.1.1.7, particularly pronounced for mAb 269, where neutralization was almost completely lost and mAb 278, which failed to reach 100% neutralization showing a maximum of only 78%.”
Quote in the paperSubstantial claimMay combine two claims.
Findingown dataThe N501Y mutation causes a marked 7-fold increase in RBD binding affinity for ACE2 due to a slower off rate, with WT RBD(501N)-ACE2 KD 75.1 nM and RBD(501Y)-ACE2 KD 10.7 nM.
“The results indicate a marked (7-fold) increase in binding affinity due to a slower off rate: WT RBD(501N)-ACE2: KD 75.1 nM (Kon 3.88E4 /Ms, Koff 2.92E-3 /s), RBD(501Y)-ACE2: KD 10.7 nM (Kon 6.38E4 /Ms, Koff 6.85E-4/s).”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Findingown dataWhen the structure was refined with an asparagine at position 501, there was strong, dispersed positive density around the side chain, consistent with the presence of a flexible tyrosine residue.
“However, when the structure was refined with an asparagine at 501, there was strong, dispersed positive density around the side chain, consistent with the presence of a flexible tyrosine residue (Figure S2).”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataThe major B.1.1.7 strain has the Δ69-70 deletion, whereas the two minor groups lack this deletion and have either wild-type or the S982A mutation.
“The major strain was the Δ69-70 B.1.1.7 strain, whereas the two minor groups lack this deletion and either had wild-type or the S982A mutation (Figure S1B).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Findingown dataPublic antibody responses including IGHV3-53 (5 potent mAbs), IGHV1-58 (4 potent mAbs), and IGHV3-66 (2 potent mAbs) were present in the RBD-specific mAb collection.
“A number of public antibody responses including IGHV3-53 (5 potent mAbs), IGHV1-58 (4 potent mAbs), and IGHV3-66 (2 potent mAbs) were present in the collection of RBD-specific mAbs”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataThe 501Y mutation in the Fab 269 complex introduces a small displacement of the L1 loop and a concomitant effect on the L3 loop, with a significant switch in Y94 position that abrogates contacts with R403 and E406 of the RBD.
“The mutation introduces a rather small displacement of the L1 loop (Figure 3D), but there is a concomitant effect of the neighboring L3 loop (Figure 3E), with a significant switch in the position of Y94, abrogating contacts with residues R403 and E406 of the RBD.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Findingown dataDuring the week of December 24, 2020, the N501Y variant represented 53% of sequenced isolates in Great Britain.
“During the week of December 24, 2020, the N501Y variant represented 53% of the sequenced isolates in Great Britain.”
Quote in the paperNot a substantial claimMay combine two claims.
Premisenone givenB.1.1.7, 501Y.V2, and P.1 all contain mutations in the ACE2 receptor binding footprint of the RBD, with N501Y common to all.
“All of these contain mutations in the ACE2 receptor binding footprint of the receptor binding domain (RBD), one in B.1.1.7, three in 501Y.V2, and three in P.1, with the N501Y mutation being common to all.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThe B.1.1.7 variant is estimated to be 30%-60% more infectious than strains encountered in the first wave.
“The B.1.1.7 variant is estimated to be 30%–60% more infectious than strains encountered in the first wave (Walker et al., 2021)”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Walker et al., 2021
Not checked in the free run.
Classified as probably not a substantial claim. May combine two claims.
Study design and conductown dataBoth Victoria passage 5 and B.1.1.7 stocks passage 2 were sequence verified to contain the expected spike protein sequence and no changes to the furin cleavage sites.
“Both Victoria passage 5 and B.1.1.7 stocks passage 2, were sequence verified to contain the expected spike protein sequence and no changes to the furin cleavage sites.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductnone givenThe study was conducted according to the principles of the Declaration of Helsinki (2008) and the International Conference on Harmonization (ICH) Good Clinical Practice (GCP) guidelines.
“The study was conducted according to the principles of the Declaration of Helsinki (2008) and the International Conference on Harmonization (ICH) Good Clinical Practice (GCP) guidelines.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown dataNeutralization assays on convalescent and vaccine serum showed that B.1.1.7 required higher serum concentrations to achieve neutralization, although there was no evidence that B.1.1.7 could evade neutralization by serum raised to early SARS-CoV-2 strains or vaccines.
“In conclusion, the neutralization assays on convalescent and vaccine serum revealed that the B.1.1.7 virus required higher concentrations of serum to achieve neutralization, although there was no evidence that the B.1.1.7 virus could evade neutralization by serum raised to early SARS-CoV-2 strains or vaccines.”
Quote in the paperSubstantial claimMay combine two claims.
InterpretationreasoningAntibodies that neutralize by ACE2 competition, even if not directly affected by the mutation, must compete with ACE2 for RBD binding, and mutations that increase ACE2 affinity will tip the equilibrium away from mAb/RBD interaction toward RBD/ACE2, making the virus more difficult to neutralize.
“However, antibodies that neutralize by ACE2 competition, even if not directly affected by the mutation, will have to compete with ACE2 for binding to the RBD, and mutations of RBD that increase the affinity of ACE2 will tip the equilibrium away from mAb/RBD interaction toward RBD/ACE2 making the virus more difficult to neutralize.”
Quote in the paperSubstantial claimMay combine two claims.
InterpretationreasoningReduced binding and neutralization were particularly marked for some, but not all, members of the public IGHV3-53 class of mAb, because the IGHV3-53-defined CDR1 and CDR2 orient the light chain close to Y501.
“The reduced binding and neutralization were particularly marked for some, but not all, members of the public IGHV3-53 class of mAb, since the IGHV3-53-defined CDR1 and CDR2 cause the antibody to orient the light chain in close proximity to Y501.”
Quote in the paperSubstantial claimMay combine two claims.
InterpretationcitationA mutation at 484 of the spike likely has a similar dual effect, and further affinity increase in ACE2 binding is possible.
“A mutation at 484 of the spike likely has a similar dual effect, and Zahradník et al. (2021) report that further affinity increase in ACE2 binding is possible.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Zahradník et al., 2021
Not checked in the free run.
Classified as probably not a substantial claim.
Study design and conductown dataThe RBD N501Y construct encodes exactly the same protein as native RBD except for the N501Y mutation, as confirmed by sequencing.
“This construct encodes exactly the same protein as native RBD except the N501Y mutation, as confirmed by sequencing.”
Quote in the paperSubstantial claimMay combine two claims.
Interpretationown dataAlthough neutralization titers against B.1.1.7 are reduced, they remain robust, and there is no evidence of vaccine escape, which bodes well for protection against B.1.1.7 by currently deployed vaccines.
“However, although neutralization titers against B.1.1.7 are reduced, they remain robust, and there is no evidence of vaccine escape, which bodes well for protection against B.1.1.7 by the vaccines currently being deployed at massive scale against SARS-CoV-2.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationThere was a correlation between ACE2 blocking and neutralization titers.
“As expected, there was a correlation between ACE2 blocking and neutralization titers”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Dejnirattisai et al., 2021 source
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenAn independent DSMB reviewed all interim safety reports for the AstraZeneca-Oxford trial.
“An independent DSMB reviewed all interim safety reports.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S4 (based). May combine two claims.
Interpretationnone givenThe N501Y mutation has the potential to increase RBD/ACE2 affinity while also disrupting the binding of potent neutralizing antibodies.
“Mutation N501Y perhaps gives the greatest concern as it has the potential to increase RBD/ACE2 affinity while also disrupting the binding of potent neutralizing antibodies (Figure 1A).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationNatural exposure and vaccination may confer protective immunity against symptomatic and severe COVID-19 via memory T cell responses.
“In addition, natural exposure and vaccination may confer protective immunity against symptomatic and severe COVID-19 via memory T cell responses (Sariol and Perlman, 2020; Altmann and Boyton, 2020).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Sariol and Perlman, 2020
Not checked in the free run.
- cites Altmann and Boyton, 2020
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationPartial or non-neutralizing antibodies may confer protection.
“indeed partial or non-neutralizing antibodies may confer protection (Henry Dunand et al., 2016).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Henry Dunand et al., 2016 source
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenWritten informed consent was obtained for all patients enrolled in the study.
“Written informed consent was obtained for all patients enrolled in the study.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown dataThe N501Y affinity increase alone might account for the selection of the N501Y mutation and an increase in transmission.
“This alone might account for the selection of the N501Y mutation and an increase in transmission.”
Quote in the paperSubstantial claim- The authors state this as an assumption: A further increase in ACE2 affinity will increase the likelihood that stochastic virus attachment events lead to localization for sufficient time to trigger internalization.
Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductown dataThe AstraZeneca-Oxford trial was sponsored by the University of Oxford and approved by a national ethics committee (South Central Berkshire Research Ethics Committee, reference 20/SC/0145 and 20/SC/0179) and a regulatory agency in the United Kingdom (the Medicines and Healthcare Products Regulatory Agency).
“The studies were sponsored by the University of Oxford (Oxford, UK) and approval obtained from a national ethics committee (South Central Berkshire Research Ethics Committee, reference 20/SC/0145 and 20/SC/0179) and a regulatory agency in the United Kingdom (the Medicines and Healthcare Products Regulatory Agency).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenThe AstraZeneca-Oxford ChAdOx1 nCoV-19 studies were registered at ISRCTN (15281137 and 89951424) and ClinicalTrials.gov (NCT04324606 and NCT04400838).
“These studies were registered at ISRCTN (15281137 and 89951424) and ClinicalTrials.gov (NCT04324606 and NCT04400838).”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown dataNeutralizing responses against the Victoria virus are less effective against B.1.1.7, and part of this effect is due to N501Y, as demonstrated by weaker binding of a number of antibodies to RBD where N501Y is the only difference.
“We have shown here that neutralizing responses against the Victoria virus are less effective against B.1.1.7 and that part of this effect is due to the N501Y mutation as demonstrated by the weaker binding of a number of antibodies to the RBD, where N501Y is the only difference.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing), S4 (based). May combine two claims.
Study design and conductnone givenConvalescent plasma and vaccine serum were taken relatively soon after acute illness or following vaccination, and it is possible that titers will drop over time to a point where they are no longer high enough to provide protection.
“Convalescent plasma and vaccine serum were taken relatively soon after acute illness or following vaccination; it is possible that titers will drop over time to a point where they are no longer high enough to provide protection.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
PremisecitationMutations in the ACE2 receptor binding domain are believed to increase affinity for ACE2.
“It is believed that these mutations in the ACE2 receptor binding domain increase the affinity for ACE2 (Zahradník et al., 2021).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Zahradník et al., 2021
Not checked in the free run.
Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductnone givenError bars are derived from curve fitting and may underestimate experimental error.
“Error bars are derived from curve fitting and may underestimate experimental error.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenThe study was approved by the Oxford Translational Gastrointestinal Unit GI Biobank Study 16/YH/0247 (REC at Yorkshire & The Humber - Sheffield).
“The study was approved by the Oxford Translational Gastrointestinal Unit GI Biobank Study 16/YH/0247 [research ethics committee (REC) at Yorkshire & The Humber – Sheffield].”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing), S4 (based).
Study design and conductnone givenThe correlates of protection from SARS-CoV-2 infection are yet to be established.
“The correlates of protection from SARS-CoV-2 infection are yet to be established.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductnone givenWritten informed consent was obtained from all participants in the AstraZeneca-Oxford trial, and the trial was conducted in accordance with the principles of the Declaration of Helsinki and Good Clinical Practice.
“Written informed consent was obtained from all participants, and the trial is being done in accordance with the principles of the Declaration of Helsinki and Good Clinical Practice.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.
Study design and conductnone givenThe in vitro neutralization assays reported here do not convey the contributions to in vivo protection provided by T cells nor the contributions of Fcγ receptor interactions and complement activation.
“The in vitro neutralization assays reported here do not convey the contributions to in vivo protection provided by T cells nor the contributions of Fcγ receptor interactions and complement activation.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown dataB.1.1.7 showed only a 5.7-fold reduction in FRNT50 for mAb 159 (Victoria 11 ng/mL, B.1.1.7 61 ng/mL), suggesting that despite the residue 144 deletion being on the edge of the antibody footprint, the binding site has not been completely disrupted.
“In this study, B.1.1.7 showed only a 5.7-fold reduction in the FRNT50 for mAb 159 (FRNT50 Victoria 11 ng/mL B.1.1.7 61 ng/mL) suggesting that despite the residue 144 deletion being on the edge of the footprint for this antibody (Dejnirattisai et al., 2021) the binding site has not been completely disrupted.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Dejnirattisai et al., 2021 source
Not checked in the free run.
The authors state this as an assumption.
A further increase in ACE2 affinity will increase the likelihood that stochastic virus attachment events lead to localization for sufficient time to trigger internalization.
“It is reasonable to assume that a further increase in affinity will increase the likelihood of the stochastic events of virus attachment resulting in localization for sufficient time to trigger, perhaps by the recruitment of additional receptors, internalization of the virus.”
The paper relies on this without support.
The higher affinity of SARS-CoV-2 for ACE2 underlies its greater transmission.
“the higher affinity for ACE2 of SARS-CoV-2 has been imputed to underlie its greater transmission.”
The paper relies on this without support.
The Pfizer vaccinees had no prior SARS-CoV-2 infection at entry.
“participants were to the best of their knowledge seronegative at entry”
“Vaccinees were Health Care Workers, based at Oxford University Hospitals NHS Foundation Trust, not known to have prior infection with SARS-C0V-2.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The impact of B.1.1.7 mutations on neutralizing antibody titers is moderate.
“In general, the impact of B.1.1.7 mutations on neutralizing antibody titers is moderate.15, 16, 17, 18,20,24”
From Impact of SARS-CoV-2 variants on the total CD4+ and CD8+ T cell reactivity in infected or vaccinated individuals (2021) · cites this paper as [18]
The neutralizing titers of convalescent and vaccine sera are reduced to B.1.351, leading to a 13-fold reduction in neutralizing titers of convalescent serum, with a number of neutralizing mAbs losing activity completely.
“The neutralizing titers of convalescent and vaccine sera are reduced to the variants with B.1.351 of most concern, leading to a 13-fold reduction in neutralizing titers of convalescent serum, with a number of neutralizing monoclonal antibodies losing activity completely (Zhou et al., 2021; Supasa et al., 2021; Dejnirattisai et al., 2021b; Shinde et al., 2021; Madhi et al., 2021; Food and Drug Adm”
From Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum (2021) · cites this paper as Supasa et al., 2021
Vaccine efficacy against B.1.1.7 is maintained.
“Conversely, vaccine efficacy against B.1.1.7 is maintained (Wang et al., 2021; Emary et al., 2021; Supasa et al., 2021).”
From Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum (2021) · cites this paper as Supasa et al., 2021
For B.1.617.2, reductions in neutralization were comparable with those seen with B.1.1.7 and P.1.
“For B.1.617.2, reductions were comparable with those seen with B.1.1.7 and P.1 (Supasa et al., 2021; Dejnirattisai et al., 2021b)”
From Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum (2021) · cites this paper as Supasa et al., 2021
A further live coronavirus neutralisation assay showed that sera from BNT162b2 and ChAdOx1 nCoV-19 vaccinees had a 2.0-3.3 times reduction in neutralisation activity against B.1.1.7 compared with the Victoria lineage.
“However, a further live coronavirus neutralisation assay showed that sera from BNT162b2 and ChAdOx1 nCoV-19 vaccinees had a 2·0–3·3 times reduction in neutralisation activity against B.1.1.7 compared with the Victoria lineage,44 in keeping with our findings.”
The Alpha variant is susceptible to neutralization by most neutralizing mAbs as well as by most plasma samples from previously infected persons.
“The Alpha variant is susceptible to neutralization by most neutralizing mAbs as well as by most plasma samples from previously infected persons 97,102,121,149,159,[203][204][205][206] (fIg.5).”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [102]
The Alpha variant has displayed 3-fold to 10-fold reduced susceptibility to approximately 15% of plasma samples from recipients of an authorized mRNA vaccine.
“The Alpha variant has displayed 3-fold to 10-fold reduced susceptibility to approximately 15% of plasma samples from recipients of an authorized mRNA vaccine 97,102,121,148,149,152,159,204,208,209 .”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [102]
In three other studies, the median reduction in neutralizing activity to the Alpha variant was between onefold and threefold.
“However, in three other studies, the median reduction in neutralizing activity was between onefold and threefold 102,214,215 .”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [102]
The NTD mutations in P.1 (L18F, T20N, P26S, D138Y, and R190S) disrupt the epitope for mAb159.
“it is clear that the NTD mutations in P.1 (L18F, T20N, P26S, D138Y, and R190S) disrupt the epitope for mAb159”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
Most other VH3-53 antibodies have direct contacts that confer susceptibility to escape by mutation to tyrosine.
“This is in contrast to the situation with most other VH3-53 antibodies, where direct contacts confer susceptibility to escape by mutation to a tyrosine (Figures 2I, 3J, and 3A; Supasa et al., 2021; Zhou et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
N501Y increased RBD-ACE2 affinity 7-fold, and the combination of 417, 484, and 501 mutations further increased affinity 19-fold compared to Wuhan.
“N501Y increased affinity 7-fold, and the combination of 417, 484, and 501 mutations further increased affinity (19-fold compared to Wuhan).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
The increase in receptor affinity may drive increased virus transmissibility, allowing the three variants to become dominant strains in the regions where they emerged.
“It seems conceivable that this increase in receptor affinity may drive increased virus transmissibility, allowing the three variants to become dominant strains in the regions where they emerged (Zhou et al., 2021; Supasa et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
Using convalescent serum, B.1.351 showed 13-fold reduction in neutralization compared to Victoria, while P.1 was only reduced 3.1-fold, comparable to B.1.1.7.
“Using convalescent serum, B.1.351 showed 13-fold reduction in neutralization compared to Victoria, while P.1 was only reduced 3.1-fold, comparable to the reduction seen with B.1.1.7, which only harbors the single N501Y change in the RBD (Zhou et al., 2021; Supasa et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
The constructs of EY6A Fab, 222 Fab, ACE2, WT RBD, B.1.1.7 and B.1.351 mutant RBD are the same as previously described.
“The constructs of EY6A Fab, 222 Fab, ACE2, WT RBD, B.1.1.7 and B.1.351 mutant RBD are the same as previously described (Dejnirattisai et al., 2021; Zhou et al., 2021; Supasa et al., 2021).”
From Antibody evasion by the P.1 strain of SARS-CoV-2 (2021) · cites this paper as Supasa et al., 2021
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Conflicting cryoprotectant descriptions for the unmutated RBD/269 crystals
MinorN501 RBD denotes the unmutated RBD. The methods say its crystals were dipped in a glycerol-containing solution, then say no cryoprotectant was used for RBD/269 crystals.
“Crystals of N501 RBD/269 Fab were mounted in loops and dipped in solution containing 25% glycerol and 75% mother liquor for a second before being frozen in liquid nitrogen prior to data collection.”
“No cryo-protectant was used for RBD/269 crystals.”
Sequence-download date precedes the analyzed isolates
MinorThe methods say the sequences were downloaded in January 2020, but the analysis includes isolates from December 2020. The stated download date cannot account for those isolates.
“All COG-UK sequences were downloaded on 24th January 2020”
“During the week of December 24, 2020, the N501Y variant represented 53% of the sequenced isolates in Great Britain.”
Cites
<i>Coot</i> : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works
<i>Phaser</i> crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
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 · see citing works
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 · see citing works
Inference of macromolecular assemblies from crystalline state.
Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,189 · see citing works
Efficacy and Safety of the mRNA-1273 SARS-CoV-2 Vaccine
Baden, L. R., El Sahly, H. M., Essink, B., Kotloff, K., Frey, S., Novak, R., Diemert, D., Spector, S. A., Rouphael, N., Creech, C. B., et al. (2021) · New England Journal of Medicine · doi:10.1056/nejmoa2035389 · Cited by 10,119 · see citing works
Liebschner, D. C., Afonine, P. V., Baker, M. L., Bunkòczi, G., Chen, V. B., Croll, T. I., Hintze, B. J., Hung, L., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 6,709 · see citing works
Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor
Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., Zhang, Q., Shi, X., Wang, Q., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2180-5 · Cited by 5,983 · see citing works
Voysey, M., Clemens, S. A. C., Madhi, S. A., Weckx, L. Y., Folegatti, P. M., Aley, P. K., Angus, B., Baillie, V. L., Barnabas, S. L., Bhorat, Q. E., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(20)32661-1 · Cited by 4,616 · see citing works
Self-citationOu, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097 · see citing works
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 · see citing works
xia2 : an expert system for macromolecular crystallography data reduction
Winter, G. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889809045701 · Cited by 1,530 · see citing works
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385 · see citing works
Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike
Liu, L., Wang, P., Nair, M. S., Yu, J., Rapp, M., Wang, Q., Luo, Y., Chan, J. F.-W., Sahi, V., Figueroa, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2571-7 · Cited by 1,349 · see citing works
Baum, A., Fulton, B. O., Wloga, E., Copin, R., Pascal, K. E., Russo, V., Giordano, S., Lanza, K., Negron, N., Ni, M., et al. (2020) · Science · doi:10.1126/science.abd0831 · Cited by 1,253 · see citing works
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · doi:10.1101/2020.12.31.425021 · Cited by 1,178 · cited 1× · see citing works
“These mutations also fall within the footprint of a number of potent neutralizing antibodies likely to afford vaccine-induced protection and of several candidate therapeutic mAbs (Cheng et al., 2021; Greaney et al., 2021; Nelson et al., 2021), thus potentially affording mutant viruses greater fitness to infect new hos…”
Greaney, A. J., Loes, A. N., Crawford, K. H. D., Starr, T. N., Malone, K. D., Chu, H. Y., & Bloom, J. D. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.02.003 · Cited by 1,178 · see citing works
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01285-x · Cited by 1,147 · see citing works
DIALS : implementation and evaluation of a new integration package
Winter, G., Waterman, D. G., Parkhurst, J. M., Brewster, A. S., Gildea, R. J., Gerstel, M., Fuentes‐Montero, L., Vollmar, M., Michels-Clark, T., Young, I. D., et al. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317017235 · Cited by 1,128 · see citing works
SARS-CoV-2 evolution during treatment of chronic infection
Kemp, S. A., Collier, D. A., Datir, R. P., Ferreira, I. A. T. M., Gayed, S., Jahun, A., Hosmillo, M., Rees-Spear, C., Mlcochova, P., Lumb, I. U., et al. (2021) · Nature · doi:10.1038/s41586-021-03291-y · Cited by 1,097 · see citing works
Transmission of SARS-CoV-2 on mink farms between humans and mink and back to humans
Munnink, B. B. O., Sikkema, R. S., Nieuwenhuijse, D. F., Molenaar, R. J., Münger, E., Molenkamp, R., van der Spek, A. N., Tolsma, P., Rietveld, A., Brouwer, M., et al. (2020) · Science · doi:10.1126/science.abe5901 · Cited by 1,087 · see citing works
Jia, H. P., Look, D. C., Shi, L., Hickey, M. A., Pewe, L. L., Netland, J., Farzan, M., Wohlford-Lenane, C., Perlman, S. M., & McCray, P. B. (2005) · Journal of Virology · doi:10.1128/jvi.79.23.14614-14621.2005 · Cited by 950 · see citing works
Barnes, C. O., West, A. P., Huey-Tubman, K. E., Hoffmann, M. A. G., Sharaf, N. G., Hoffman, P. R., Koranda, N., Gristick, H. B., Gaebler, C., Muecksch, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.025 · Cited by 795 · see citing works
Adaptation of SARS-CoV-2 in BALB/c mice for testing vaccine efficacy
Gu, H., Chen, Q., Yang, G., He, L., Fan, H., Deng, Y.-Q., Wang, Y., Teng, Y., Zhao, Z., Cui, Y., et al. (2020) · Science · doi:10.1126/science.abc4730 · Cited by 762 · see citing works
A time- and cost-efficient system for high-level protein production in mammalian cells
Aricescu, A. R., Lu, W., & Jones, E. Y. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029799 · Cited by 746 · see citing works
Structural basis of a shared antibody response to SARS-CoV-2
Yuan, M., Liu, H., Wu, N. C., Lee, C.-C. D., Zhu, X., Zhao, F., Huang, D., Yu, W., Hua, Y., Tien, H., et al. (2020) · Science · doi:10.1126/science.abd2321 · Cited by 589 · see citing works
Cerutti, G., Guo, Y.-C., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E., Yu, J., Bahna, F., Bimela, J. S., et al. (2021) · bioRxiv · doi:10.1101/2021.01.10.426120 · Cited by 539 · see citing works
Cerutti, G., Guo, Y., Zhou, T., Gorman, J., Lee, M., Rapp, M., Reddem, E. R., Yu, J., Bahna, F., Bimela, J., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.03.005 · Cited by 519 · see citing works
Denison, M. R., Graham, R. L., Donaldson, E., Eckerle, L. D., & Baric, R. S. (2011) · RNA Biology · doi:10.4161/rna.8.2.15013 · Cited by 490 · see citing works
Zahradník, J., Marciano, S., Shemesh, M., Zoler, E., Chiaravalli, J., Meyer, B., Rudich, Y., Dym, O., Elad, N., & Schreiber, G. (2021) · doi:10.1101/2021.01.06.425392 · Cited by 458 · cited 4× · see citing works
“As noted by Zahradnı́k et al. (2021) in a situation where public health measures reduce R0 to below 1, there will be selective pressure to increase receptor affinity.”
BackgroundInfluentialCrystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
Stuart, D. I., Levine, M., Muirhead, H., & STAMMERS, D. K. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90416-9 · Cited by 440 · see citing works
Self-citationSARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
Zahradník, J., Marciano, S., Shemesh, M., Zoler, E., Harari, D., Chiaravalli, J., Meyer, B., Rudich, Y., Li, C., Marton, I., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00954-4 · Cited by 440 · see citing works
Coronavirus RNA Proofreading: Molecular Basis and Therapeutic Targeting
Robson, F., Khan, K. S., Le, T. K., Paris, C., Demirbag, S., Barfuss, P., Rocchi, P., & Ng, W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.027 · Cited by 398 · see citing works
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 397 · see citing works
The 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 · see citing works
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) · doi:10.1101/2021.01.19.427324 · Cited by 361 · see citing works
Neutralization 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 317 · see citing works
Self-citationLessons for COVID-19 immunity from other coronavirus infections
Sariol, A., & Perlman, S. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.005 · Cited by 317 · see citing works
Caly, L., Druce, J. D., Roberts, J., Bond, K. A., Tran, T., Kostecki, R., Yoga, Y., Naughton, W., Taiaroa, G., Seemann, T., et al. (2020) · The Medical Journal of Australia · doi:10.5694/mja2.50569 · Cited by 305 · see citing works
Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient
Zhou, D., Duyvesteyn, H. M. E., Chen, C.-P., Huang, C.-G., Chen, T.-H., Shih, S.-R., Lin, Y.-C., Cheng, C.-Y., Cheng, S.-H., Huang, Y.-C., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0480-y · Cited by 274 · see citing works
Self-citationHenry Dunand, C. J., Leon, P. E., Huang, M., Choi, A., Chromikova, V., Ho, I. Y., Tan, G. S., Cruz, J., Hirsh, A., Zheng, N.-Y., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.05.014 · Cited by 268 · see citing works
SARS-CoV-2 T cell immunity: Specificity, function, durability, and role in protection
Altmann, D., & Boyton, R. (2020) · Science immunology · doi:10.1126/sciimmunol.abd6160 · Cited by 255 · see citing works
Neutralising antibodies in Spike mediated SARS-CoV-2 adaptationPreprint
Kemp, S. A., Collier, D. A., Datir, R. P., et al. (2020) · medRxiv · doi:10.1101/2020.12.05.20241927 · Cited by 180 · see citing works
Zhu, X. Q., Mannar, D., Srivastava, S. S., Berezuk, A., Demers, J., Saville, J. W., Leopold, K., Li, W., Dimitrov, D. S., Tuttle, K. S., et al. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001237 · Cited by 176 · see citing works
Nelson, G., Buzko, O. V., Spilman, P., Niazi, K., Rabizadeh, S., & Soon‐Shiong, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.13.426558 · Cited by 175 · see citing works
An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain
Wu, N. C., Yuan, M., Liu, H., Lee, C.-C. D., Zhu, X., Bangaru, S., Torres, J. L., Caniels, T. G., Brouwer, P. J. M., van Gils, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108274 · Cited by 157 · see citing works
Recombinant vaccines for COVID-19
Yadav, T., Srivastava, N., Mishra, G., Dhama, K., Kumar, S., Puri, B., & Saxena, S. K. (2020) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2020.1820808 · Cited by 105 · see citing works
Walter, T. S., Diprose, J. M., Brown, J., Pickford, M. G., Owens, R. J., Stuart, D. I., & Harlos, K. (2003) · Journal of Applied Crystallography · doi:10.1107/s0021889803001997 · Cited by 101 · see citing works
Self-citationYang, L., Liu, W., Yu, X., Wu, M., Reichert, J. M., & Ho, M. (2020) · Antibody Therapeutics · doi:10.1093/abt/tbaa020 · Cited by 101 · see citing works
Coronavirus RNA Proofreading: Molecular Basis and Therapeutic Targeting
Robson, F., Khan, K. S., Le, T. K., Paris, C., Demirbag, S., Barfuss, P., Rocchi, P., & Ng, W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.048 · Cited by 73 · see citing works
Increased infections, but not viral burden, with a new SARS-CoV-2 variant
Walker, A. S., Vihta, K.-D., Gethings, O., Pritchard, E., Jones, J., House, T., Bell, I., Bell, J. I., Newton, J. N., Farrar, J., et al. (2021) · doi:10.1101/2021.01.13.21249721 · Cited by 58 · see citing works
Self-citationCheng, M. H., Krieger, J., Kaynak, B., Arditi, M., & Bahar, İ. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.10.426143 · Cited by 58 · see citing works
Nettleship, J. E., Ren, J., Rahman, N., Berrow, N. S., Hatherley, D., Barclay, A. N., & Owens, R. J. (2008) · Protein Expression and Purification · doi:10.1016/j.pep.2008.06.017 · Cited by 48 · see citing works
Self-citationHighly conserved binding region of ACE2 as a receptor for SARS-CoV-2 between humans and mammals
Hayashi, T., Abiko, K., Mandai, M., Yaegashi, N., & Konishi, I. (2020) · Veterinary Quarterly · doi:10.1080/01652176.2020.1823522 · Cited by 47 · see citing works
Zhu, X., Mannar, D., Srivastava, S. S., Berezuk, A. M., Demers, J.-P., Saville, J. W., Leopold, K., Li, W., Dimitrov, D. S., Tuttle, K. S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.11.426269 · Cited by 12 · see citing works
Kröger, M., & Schlickeiser, R. (2021) · Royal Society Open Science · doi:10.1098/rsos.211379 · Cited by 11 · see citing works
Kröger, M., & Schlickeiser, R. (2021) · Preprints.org · doi:10.20944/preprints202101.0449.v1 · Cited by 4 · see citing works
SARS-CoV-2 501Y.V2 escapes neutralization by South African COVID-19 donor plasma
Wibmer, C. K., Ayres, F., Hermanus, T., Madzivhandila, M., Kgagudi, P., Oosthuysen, B., Lambson, B. E., de Oliveira, T., Vermeulen, M., van der Berg, K., et al. (2021) · doi:10.1101/2021.01.18.427166
Flagged first, then by citations
2 of the 60 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Nelson, 2021, bioRxiv
- Zhu, 2021, Cryo-EM Structure of the N501Y SARS-CoV-2 Spike Protein in Complex with a Potent Neutralizing Antibody, bioRxiv
Cited by
Sorted by citations
The biological and clinical significance of emerging SARS-CoV-2 variants
Tao, K., Tzou, P. L., Nouhin, J., Gupta, R. K., de Oliveira, T., Kosakovsky Pond, S. L., Fera, D., & Shafer, R. W. (2021) · Nature Reviews Genetics · doi:10.1038/s41576-021-00408-x · Cited by 1,009 · see citing works
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.046 · Cited by 930 · see citing works
Self-citationFiolet, T., Kherabi, Y., MacDonald, C.-J., Ghosn, J., & Peiffer-Smadja, N. (2022) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2021.10.005 · Cited by 911 · see citing works
Effect of 2 Inactivated SARS-CoV-2 Vaccines on Symptomatic COVID-19 Infection in Adults
Kaabi, N. A. M. A., Zhang, Y., Xia, S., Yang, Y., AlQahtani, M., Abdulrazzaq, N. M., Nusair, M. A., Hassany, M., Jawad, J. S., Abdalla, J., et al. (2021) · JAMA · doi:10.1001/jama.2021.8565 · Cited by 757 · see citing works
Self-citationAntibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum
Tuekprakhon, A., Nutalai, R., Dijokaite-Guraliuc, A., Zhou, D., Ginn, H. M., Selvaraj, M., Liu, C., Mentzer, A. J., Supasa, P., Duyvesteyn, H. M. E., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.005 · Cited by 677 · see citing works
Self-citationTarke, A., Sidney, J., Methot, N., Yu, E. D., Zhang, Y., Dan, J. M., Goodwin, B., Rubiro, P., Sutherland, A., Wang, E., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100355 · Cited by 706 · see citing works
Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum
Liu, C., Ginn, H. M., Dejnirattisai, W., Supasa, P., Wang, B., Tuekprakhon, A., Nutalai, R., Zhou, D., Mentzer, A. J., Zhao, Y., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.020 · Cited by 669 · see citing works
Self-citationAntibody evasion by the P.1 strain of SARS-CoV-2
Dejnirattisai, W., Zhou, D., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.055 · Cited by 583 · see citing works
Self-citationEmary, K. R. W., Golubchik, T., Aley, P. K., Ariani, C. V., Angus, B., Bibi, S., Blane, B., Bonsall, D., Cicconi, P., Charlton, S., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00628-0 · Cited by 603 · see citing works
Self-citationSARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity
Motozono, C., Toyoda, M., Zahradnik, J., Saito, A., Nasser, H., Tan, T. S., Ngare, I., Kimura, I., Uriu, K., Kosugi, Y., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.06.006 · Cited by 586 · see citing works
Cromer, D., Steain, M., Reynaldi, A., Schlub, T. E., Wheatley, A. K., Juno, J. A., Kent, S. J., Triccas, J. A., Khoury, D. S., & Davenport, M. P. (2022) · The Lancet Microbe · doi:10.1016/s2666-5247(21)00267-6 · Cited by 590 · see citing works
Abani, O., Abbas, A. H., Abbas, F., Abbas, M. A., Abbasi, S., Abbass, H., Abbott, A., Abdallah, N., Abdelaziz, A., Abdelfattah, M., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00897-7 · Cited by 493 · see citing works
Barros-Martins, J., Hammerschmidt, S. I., Cossmann, A., Odak, I., Stankov, M. V., Morillas Ramos, G., Dopfer-Jablonka, A., Heidemann, A., Ritter, C., Friedrichsen, M., et al. (2021) · Nature Medicine · doi:10.1038/s41591-021-01449-9 · Cited by 425 · see citing works
COVID-19 vaccine development: milestones, lessons and prospects
Li, M., Wang, H., Tian, L., Pang, Z., Yang, Q., Huang, T., Fan, J., Song, L., Tong, Y., & Fan, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00996-y · Cited by 448 · see citing works
Prior SARS-CoV-2 infection rescues B and T cell responses to variants after first vaccine dose
Reynolds, C. J., Pade, C., Gibbons, J. M., Butler, D. K., Otter, A. D., Menacho, K., Fontana, M., Smit, A., Sackville-West, J. E., Cutino-Moguel, T., et al. (2021) · Science · doi:10.1126/science.abh1282 · Cited by 338 · see citing works
Barton, M. I., MacGowan, S., Kutuzov, M. A., Dushek, O., Barton, G., & van der Merwe, P. A. (2021) · eLife · doi:10.7554/elife.70658 · Cited by 301 · see citing works
Inflammasome activation at the crux of severe COVID-19
Vora, S. M., Lieberman, J., & Wu, H. (2021) · Nature reviews. Immunology · doi:10.1038/s41577-021-00588-x · Cited by 323 · see citing works
Immunogenicity of standard and extended dosing intervals of BNT162b2 mRNA vaccine
Payne, R. P., Longet, S., Austin, J. A., Skelly, D. T., Dejnirattisai, W., Adele, S., Meardon, N., Faustini, S., Al-Taei, S., Moore, S. C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.10.011 · Cited by 322 · see citing works
Self-citationAn infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Liu, Y., Soh, W. T., Kishikawa, J.-I., Hirose, M., Nakayama, E. E., Li, S., Sasai, M., Suzuki, T., Tada, A., Arakawa, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.032 · Cited by 269 · see citing works
Zeng, B., Gao, L., Zhou, Q., Yu, K., & Sun, F. (2022) · BMC Medicine · doi:10.1186/s12916-022-02397-y · Cited by 267 · see citing works
A Comprehensive Review of COVID-19 Virology, Vaccines, Variants, and Therapeutics
Forchette, L., Sebastian, W., & Liu, T. (2021) · Current Medical Science · doi:10.1007/s11596-021-2395-1 · Cited by 260 · see citing works
Hoffmann, M., Hofmann-Winkler, H., Krüger, N., Kempf, A., Nehlmeier, I., Graichen, L., Arora, P., Sidarovich, A., Moldenhauer, A.-S., Winkler, M. S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109415 · Cited by 258 · see citing works
SARS-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
Wei, J., Pouwels, K. B., Stoesser, N. E., Matthews, P. C., Diamond, I. D., Studley, R., Rourke, E. D., Cook, D., Bell, J. I., Newton, J. N., et al. (2022) · Nature Medicine · doi:10.1038/s41591-022-01721-6 · Cited by 236 · see citing works
Self-citationFrater, J., Ewer, K., Ogbe, A., Pace, M., Adele, S., Adland, E., Alagaratnam, J., Aley, P. K., Ali, M., Ansari, M. A., et al. (2021) · The Lancet HIV · doi:10.1016/s2352-3018(21)00103-x · Cited by 223 · see citing works
Self-citationSARS-COV-2 Variants: Differences and Potential of Immune Evasion
Hirabara, S. M., Serdan, T. D. A., Gorjão, R., Masi, L. N., Pithon‐Curi, T. C., Covas, D. T., Curi, R., & Durigon, E. L. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.781429 · Cited by 216 · see citing works
Avendaño, C., Ramos, A., Múñez, E., Ruíz‐Antorán, B., de Molina, R. M., Torres, F., Fernández‐Cruz, A., Callejas-Díaz, A., Calderón, J., Payares‐Herrera, C., et al. (2021) · Journal of Clinical Investigation · doi:10.1172/jci152740 · Cited by 196 · see citing works
The Impact of Evolving SARS-CoV-2 Mutations and Variants on COVID-19 Vaccines
McLean, G. R., Kamil, J. P., Lee, B., Moore, P. L., Schulz, T. F., Muik, A., Şahin, U., Türeci, Ö., & Pather, S. (2022) · mBio · doi:10.1128/mbio.02979-21 · Cited by 190 · see citing works
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Lazarević, I., Pravica, V., Miljanovic, D., & Cupic, M. D. (2021) · Viruses · doi:10.3390/v13071192 · Cited by 188 · see citing works
Effects of SARS-CoV-2 variants on vaccine efficacy and response strategies
Bian, L., Gao, F., Zhang, J., He, Q., Mao, Q., Xu, M., & Liang, Z. (2021) · Expert Review of Vaccines · doi:10.1080/14760584.2021.1903879 · Cited by 181 · see citing works
Wang, Y., Liu, C., Zhang, C., Wang, Y., Qin, H., Xu, S., Li, Z., Yang, Y. P., Huang, Z. W., & Cong, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-28528-w · Cited by 170 · see citing works
Self-citationThe role of high cholesterol in SARS-CoV-2 infectivity
Wang, H., Yuan, Z., Pavel, M. A., Jablonski, S. M., Jablonski, J. A., Hobson, R. J., Valente, S. T., Reddy, C. B., & Hansen, S. B. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104763 · Cited by 177 · see citing works
Potent cross-reactive antibodies following Omicron breakthrough in vaccinees
Nutalai, R., Zhou, D., Tuekprakhon, A., Ginn, H. M., Supasa, P., Liu, C., Huo, J., Mentzer, A. J., Duyvesteyn, H. M. E., Dijokaite-Guraliuc, A., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.014 · Cited by 164 · see citing works
Self-citationWoldemeskel, B. A., Garliss, C. C., & Blankson, J. N. (2021) · Journal of Clinical Investigation · doi:10.1172/jci149335 · Cited by 175 · see citing works
Mahil, S. K., Bechman, K., Raharja, A., Domingo‐Vila, C., Baudry, D., Brown, M. A., Cope, A. P., Dasandi, T., Graham, C., Lechmere, T., et al. (2021) · The Lancet Rheumatology · doi:10.1016/s2665-9913(21)00212-5 · Cited by 162 · see citing works
Progress and Challenges in Targeting the SARS-CoV-2 Papain-like Protease
Tan, H., Hu, Y., Jadhav, P. D., Tan, B., & Wang, J. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00303 · Cited by 162 · see citing works
Huo, J., Mikolajek, H., Bas, A. L., Clark, J., Sharma, P., Kipar, A., Dormon, J., Norman, C. S., Weckener, M., Clare, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25480-z · Cited by 146 · see citing works
Self-citationGraham, 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
Self-citationJawad, B., Adhikari, P., Podgornik, R., & Ching, W. Y. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00560 · Cited by 148 · see citing works
Chakraborty, C., Sharma, A. R., Bhattacharya, M., & Lee, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.801522 · Cited by 150 · see citing works
Mapping SARS-CoV-2 antigenic relationships and serological responses
Wilks, S. H., Mühlemann, B., Shen, X., Türeli, S., LeGresley, E. B., Netzl, A., Caniza, M. A., Chacaltana-Huarcaya, J. N., Corman, V. M., Daniell, X. G., et al. (2023) · Science · doi:10.1126/science.adj0070 · Cited by 134 · see citing works
From delta to Omicron: S1-RBD/S2 mutation/deletion equilibrium in SARS-CoV-2 defined variants
PAPANIKOLAOU, V. S., Chrysovergis, A., Ragos, V., Tsiambas, E., Katsinis, S., Manoli, A., Papouliakos, S. M., Roukas, D., Mastronikolis, S. N., Peschos, D., et al. (2022) · Gene · doi:10.1016/j.gene.2021.146134 · Cited by 142 · see citing works
Cytokine storm in COVID-19: from viral infection to immune responses, diagnosis and therapy
Jiang, Y.-Z., Rubin, L., Peng, T., Liu, L., Xing, X., Lazarovici, P., & Zheng, W. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.59272 · Cited by 141 · see citing works
SARS-CoV-2 Neutralizing Antibodies for COVID-19 Prevention and Treatment
Li, D., Sempowski, G. D., Saunders, K. O., Acharya, P., & Haynes, B. F. (2021) · Annual Review of Medicine · doi:10.1146/annurev-med-042420-113838 · Cited by 132 · see citing works
Molecular characteristics, immune evasion, and impact of SARS-CoV-2 variants
Sun, C., Xie, C., Bu, G., Zhong, L., & Zeng, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01039-2 · Cited by 139 · see citing works
Anti-spike antibody response to natural SARS-CoV-2 infection in the general population
Wei, J., Matthews, P. C., Stoesser, N. E., Maddox, T., Lorenzi, L., Studley, R., Bell, J. I., Newton, J. N., Farrar, J., Diamond, I. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26479-2 · Cited by 131 · see citing works
Self-citationMoriyama, S., Adachi, Y., Sato, T., Tonouchi, K., Sun, L., Fukushi, S., Yamada, S., Kinoshita, H., Nojima, K., Kanno, T., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.06.015 · Cited by 133 · see citing works
Sokal, A., Spaeth, G. B., Fernández, I., Broketa, M., Azzaoui, I., Selle, A. D. L., Vandenberghe, A., Fourati, S., Roeser, A., Meola, A., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.09.011 · Cited by 128 · see citing works
Chen, J., Wang, P., Yuan, L., Zhang, L., Zhang, L., Zhao, H. J., Chen, C., Chen, Y., Han, J., Jia, J., et al. (2022) · 中国科学通报:英文版 · doi:10.1016/j.scib.2022.05.018 · Cited by 130 · see citing works
Vaccine-induced systemic and mucosal T cell immunity to SARS-CoV-2 viral variants
Kingstad-Bakke, B. A., Lee, W., Chandrasekar, S., Gasper, D. J., Salas-Quinchucua, C., Cleven, T., Sullivan, J. A., Talaat, A. M., Osorio, J. E., & Suresh, M. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2118312119 · Cited by 119 · see citing works
Kapłonek, P., Fischinger, S., Cizmeci, D., Bartsch, Y. C., Kang, J., Burke, J. S., Shin, S. A., Dayal, D., Martin, P., Mann, C. J., et al. (2022) · Immunity · doi:10.1016/j.immuni.2022.01.001 · Cited by 111 · see citing works
Emerging SARS-CoV-2 Variants of Concern (VOCs): An Impending Global Crisis
Thye, A. Y.-K., Law, J. W., Pusparajah, P., Letchumanan, V., Chan, K., & Lee, L. (2021) · Biomedicines · doi:10.3390/biomedicines9101303 · Cited by 116 · see citing works
Therapeutic 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
Chen, X., Chen, Z., Azman, A. S., Sun, R., Lu, W., Zheng, N., Zhou, J., Wu, Q., Deng, X., Zhao, Z., et al. (2022) · Clinical Infectious Diseases · doi:10.1093/cid/ciab646 · Cited by 113 · see citing works
Mutations 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
Caniels, T. G., Bontjer, I., van der Straten, K., Poniman, M., Burger, J. A., Appelman, B., Lavell, A. H. A., Oomen, M., Godeke, G.-J., Valle, C., et al. (2021) · Science Advances · doi:10.1126/sciadv.abj5365 · Cited by 105 · see citing works
Gushchin, V. А., Dolzhikova, I. V., Shchetinin, A. M., Odintsova, A. S., Siniavin, A. E., Nikiforova, M. A., Pochtovyi, A. A., Shidlovskaya, E. V., Kuznetsova, N. A., Burgasova, O., et al. (2021) · Vaccines · doi:10.3390/vaccines9070779 · Cited by 109 · see citing works
Yang, Y., Yang, M.-H., Peng, Y., Liang, Y.-J., Wei, J.-L., Xing, L., Guo, L., Li, X.-H., Li, J., Wang, J., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-021-01051-2 · Cited by 104 · see citing works
Taft, J. M., Weber, C. R., Gao, B., Ehling, R. A., Han, J., Frei, L., Metcalfe, S. W., Overath, M. D., Yermanos, A., Kelton, W., et al. (2022) · Cell · doi:10.1016/j.cell.2022.08.024 · Cited by 113 · see citing works
Evolution of enhanced innate immune evasion by the SARS-CoV-2 B.1.1.7 UK variant
Thorne, L. G., Bouhaddou, M., Reuschl, A.-K., Zuliani-Alvarez, L., Polacco, B., Pelin, A., Batra, J., Whelan, M. V. X., Ummadi, M., Rojc, A., et al. (2021) · doi:10.1101/2021.06.06.446826 · Cited by 91 · see citing works
Mutations in SARS-CoV-2: Insights on structure, variants, vaccines, and biomedical interventions
Abulsoud, A. I., El‐Husseiny, H. M., El-Husseiny, A. A., El‐Mahdy, H. A., Ismail, A., Elkhawaga, S. Y., Khidr, E. G., Fathi, D., Mady, E. A., Najda, A., et al. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113977 · Cited by 108 · see citing works
Dupont, L., Snell, L., Graham, C., Seow, J., Merrick, B., Lechmere, T., Maguire, T., Hallett, S. R., Pickering, S., Charalampous, T., et al. (2021) · Nature Microbiology · doi:10.1038/s41564-021-00974-0 · Cited by 98 · see citing works
The real-life impact of vaccination on COVID-19 mortality in Europe and Israel
Jabłońska, K., Aballéa, S., & Toumi, M. (2021) · Public Health · doi:10.1016/j.puhe.2021.07.037 · Cited by 103 · see citing works
Swanson, P. A., Padilla, M., Hoyland, W., McGlinchey, K., Fields, P., Bibi, S., Faust, S. N., McDermott, A. B., Lambe, T., Pollard, A. J., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj7211 · Cited by 104 · see citing works
Self-citationKim, S., Liu, Y., Ziarnik, M., Seo, S., Cao, Y., Zhang, X. F., & Im, W. (2022) · Journal of Computational Chemistry · doi:10.1002/jcc.27025 · Cited by 99 · see citing works
Gupta, N., Kaur, H., Yadav, P., Mukhopadhyay, L., Sahay, R., Kumar, A., Nyayanit, D. A., Shete, A., Patil, S., Majumdar, T., et al. (2021) · Viruses · doi:10.3390/v13091782 · Cited by 67 · see citing works
Population impact of SARS-CoV-2 variants with enhanced transmissibility and/or partial immune escape
Bushman, M., Kahn, R. J., Taylor, B. P., Lipsitch, M., & Hanage, W. P. (2021) · Cell · doi:10.1016/j.cell.2021.11.026 · Cited by 90 · see citing works
Evaluation of Cell-Based and Surrogate SARS-CoV-2 Neutralization Assays
Sholukh, A. M., Fiore-Gartland, A., Ford, E. S., Miner, M. D., Hou, Y., Tse, L.-P. V., Kaiser, H., Zhu, H., Lu, J. Y. C., Madarampalli, B., et al. (2021) · Journal of Clinical Microbiology · doi:10.1128/jcm.00527-21 · Cited by 87 · see citing works
Thiruvengadam, R., Awasthi, A., Medigeshi, G., Bhattacharya, S., Mani, S., Sivasubbu, S., Shrivastava, T., Samal, S., Rathna Murugesan, D., Koundinya Desiraju, B., et al. (2022) · The Lancet Infectious Diseases · doi:10.1016/s1473-3099(21)00680-0 · Cited by 96 · see citing works
Bertoglio, F., Fühner, V., Ruschig, M., Heine, P. A., Abassi, L., Klünemann, T., Rand, U., Meier, D., Langreder, N., Steinke, S., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109433 · Cited by 96 · see citing works
Saville, 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
Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain
Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75 · see citing works
Salleh, M. Z., Derrick, J. P., & Deris, Z. Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147425 · Cited by 79 · see citing works
Broadly-Neutralizing Antibodies Against Emerging SARS-CoV-2 Variants
Shrestha, L. B., Tedla, N. T., & Bull, R. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.752003 · Cited by 76 · see citing works
Emerging SARS-CoV-2 Variants: Genetic Variability and Clinical Implications
Dubey, A., Choudhary, S., Kumar, P., & Tomar, S. (2021) · Current Microbiology · doi:10.1007/s00284-021-02724-1 · Cited by 79 · see citing works
Structural basis for continued antibody evasion by the SARS-CoV-2 receptor-binding domain
Nabel, K., Clark, S., Shankar, S., Pan, J., Clark, L., Yang, P., Coscia, A., McKay, L. G. A., Varnum, H., Brusic, V., et al. (2021) · Science · doi:10.1126/science.abl6251 · Cited by 84 · see citing works
Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein
Calvaresi, V., Wrobel, A. G., Toporowska, J., Hammerschmid, D., Doores, K. J., Bradshaw, R. T., Parsons, R. B., Benton, D. J., Roustan, C., Reading, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36745-0 · Cited by 82 · see citing works
Rotondo, J., Martini, F., Maritati, M., Mazziotta, C., Mauro, G. D., Lanzillotti, C., Barp, N., Gallerani, A., Tognon, M., & Contini, C. (2021) · Viruses · doi:10.3390/v13091687 · Cited by 67 · see citing works
Emergence and phenotypic characterization of the global SARS-CoV-2 C.1.2 lineage
Scheepers, C., Everatt, J., Amoako, D. G., Tegally, H., Wibmer, C. K., Mnguni, A., Ismail, A., Mahlangu, B., Lambson, B. E., Richardson, S. I., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29579-9 · Cited by 75 · see citing works
Zollner, A., Watschinger, C., Rössler, A., Farcet, M. R., Penner, A., Böhm, V., Zollner-Kiechl, S., Stampfel, G., Hintenberger, R., Tilg, H., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103539 · Cited by 75 · see citing works
Direct comparison of antibody responses to four SARS-CoV-2 vaccines in Mongolia
Dashdorj, N., Wirz, O. F., Röltgen, K., Haraguchi, E., Buzzanco, A. S., Sibai, M., Wang, H., Miller, J. A., Solis, D., Sahoo, M. K., et al. (2021) · Cell Host & Microbe · doi:10.1016/j.chom.2021.11.004 · Cited by 76 · see citing works
Brown, J. C., Goldhill, D. H., Zhou, J., Peacock, T. P., Frise, R., Goonawardane, N., Baillon, L., Kugathasan, R., Pinto, A., McKay, P. F., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.24.432576 · Cited by 68 · see citing works
Xue, S., Han, Y., Wu, F., & Wang, Q. (2024) · Protein & Cell · doi:10.1093/procel/pwae007 · Cited by 72 · see citing works
Lumley, S., Rodger, G., Constantinides, B., Sanderson, N. D., Chau, K., Street, T. L., O’Donnell, D., Howarth, A., Hatch, S. B., Marsden, B. D., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab608 · Cited by 70 · see citing works
Self-citationZhang, H., Deng, S., Ren, L., Zheng, P., Hu, X., Jin, T., & Tan, X. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109708 · Cited by 68 · see citing works
SARS-CoV-2 variants, immune escape, and countermeasures
Zhang, Y., Zhang, H. C., & Zhang, W. (2022) · Frontiers of Medicine · doi:10.1007/s11684-021-0906-x · Cited by 70 · see citing works
Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responsesPreprint
Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.03.471045 · Cited by 69 · see citing works
Self-citationNoori, M., Nejadghaderi, S. A., Arshi, S., Carson‐Chahhoud, K., Ansarin, K., Kolahi, A., & Safiri, S. (2021) · Reviews in Medical Virology · doi:10.1002/rmv.2277 · Cited by 64 · see citing works
Wang, Z., Zhou, P., Muecksch, F., Cho, A., Tanfous, T. B., Canis, M., Witte, L., Johnson, B. A., Raspe, R., Schmidt, F., et al. (2022) · The Journal of Experimental Medicine · doi:10.1084/jem.20221006 · Cited by 66 · see citing works
The RECOVERY Collaborative Group, Horby, P., Estcourt, L. J., Peto, L., Emberson, J., Staplin, N., Spata, E., Pessoa-Amorim, G., Campbell, M. R., Roddick, A., et al. (2021) · medRxiv · doi:10.1101/2021.03.09.21252736 · Cited by 69 · see citing works
Controversy surrounding the Sputnik V vaccine
Cazzola, M., Rogliani, P., Mazzeo, F., & Matera, M. G. (2021) · Respiratory Medicine · doi:10.1016/j.rmed.2021.106569 · Cited by 66 · see citing works
Adjobimey, T., Meyer, J., Sollberg, L., Bawolt, M., Berens, C., Kovačević, P., Trudić, A., Parčina, M., & Hoerauf, A. M. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.917905 · Cited by 64 · see citing works
SARS-CoV-2’s Variants of Concern: A Brief Characterization
Scovino, A. M., Dahab, E. C., Vieira, G. F., Freire‐de‐Lima, L., Freire-de-Lima, C. G., & Morrot, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.834098 · Cited by 64 · see citing works
The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants
Liu, C., Zhou, D.-M., Nutalai, R., Duyvesteyn, H., Tuekprakhon, A., Ginn, H., Dejnirattisai, W., Supasa, P., Mentzer, A., Wang, B.-B., et al. (2021) · Cell Host and Microbe · doi:10.1016/j.chom.2021.11.013 · Cited by 65 · see citing works
Self-citationTargeting conserved N-glycosylation blocks SARS-CoV-2 variant infection in vitro
Huang, H., Lai, Y., Liao, C., Wang, F.-Y., Huang, K.-B., Lee, I., Chou, W., Wang, S., Wang, L., Hsu, J.-M., et al. (2021) · EBioMedicine · doi:10.1016/j.ebiom.2021.103712 · Cited by 61 · see citing works
Assawakosri, S., Kanokudom, S., Suntronwong, N., Auphimai, C., Nilyanimit, P., Vichaiwattana, P., Thongmee, T., Duangchinda, T., Chantima, W., Pakchotanon, P., et al. (2022) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiac092 · Cited by 59 · see citing works
Self-citationBanho, C. Á., Sacchetto, L., Campos, G. R. F., Bittar, C., Possebon, F. S., Ullmann, L. S., Marques, B. D. C., da Silva, G. C. D., Moraes, M. M., Parra, M. C. P., et al. (2022) · Communications Medicine · doi:10.1038/s43856-022-00108-5 · Cited by 63 · see citing works
SARS-CoV-2 Variants and Their Relevant Mutational Profiles: Update Summer 2021
Alkhatib, M., Svicher, V., Salpini, R., Ambrosio, F. A., Bellocchi, M. C., Carioti, L., Piermatteo, L., Scutari, R., Costa, G., Artese, A., et al. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.01096-21 · Cited by 61 · see citing works
Mandolo, J., Msefula, J., Henrion, M. Y. R., Brown, C., Moyo, B., Samon, A., Moyo-Gwete, T., Makhado, Z., Ayres, F., Motlou, T., et al. (2021) · BMC Medicine · doi:10.1186/s12916-021-02187-y · Cited by 61 · see citing works
“previous studies showing that homologous convalescent sera retain higher in vitro neutralisation potency than heterologous convalescent sera against the infecting virus [16, 21, 24, 25].”
BackgroundOnodera, T., Kita, S., Adachi, Y., Moriyama, S., Sato, A., Nomura, T., Sakakibara, S., Inoue, T., Tadokoro, T., Anraku, Y., et al. (2021) · Immunity · doi:10.1016/j.immuni.2021.08.025 · Cited by 56 · see citing works
- Authors
- Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., Wang, B., Paesen, G. C., Slon-Campos, J., López-Camacho, C., Hallis, B., Coombes, N., Bewley, K. R., Charlton, S., Walter, T. S., Barnes, E., Dunachie, S. J., Skelly, D., Lumley, S. F., Baker, N., Shaik, I., Humphries, H. E., Godwin, K., Gent, N., Sienkiewicz, A., Dold, C., Levin, R., Dong, T., Pollard, A. J., Knight, J. C., Klenerman, P., Crook, D., Lambe, T., Clutterbuck, E., Bibi, S., Flaxman, A., Bittaye, M., Belij-Rammerstorfer, S., Gilbert, S., Hall, D. R., Williams, M. A., Paterson, N. G., James, W., Carroll, M. W., Fry, E. E., Mongkolsapaya, J., Ren, J., Stuart, D. I., & Screaton, G. R.
- Affiliations
- Centre for Human Genetics (GB)
- Diamond Light Source (GB)
- Public Health England (GB)
- University of Oxford (GB)
- Worthing Hospital (GB)
- Siriraj Hospital (TH)
- Corresponding author
- Mongkolsapaya, Juthathip
- Ren, Jingshan
- Stuart, David I.
- Screaton, Gavin R.
- ORCID
- Supasa, Piyada
- Zhou, Daming
- Liu, Chang
- Mentzer, Alexander J.
- Ginn, Helen M.
- Zhao, Yuguang
- Duyvesteyn, Helen M.E.
- Nutalai, Rungtiwa
- Tuekprakhon, Aekkachai
- Wang, Beibei
- Paesen, Guido C.
- Slon-Campos, Jose
- López-Camacho, César
- Hallis, Bassam
- Coombes, Naomi
- Bewley, Kevin R.
- Charlton, Sue
- Walter, Thomas S.
- Barnes, Eleanor
- Dunachie, Susanna J.
- Skelly, Donal
- Lumley, Sheila F.
- Baker, Natalie
- Shaik, Imam
- Humphries, Holly E.
- Gent, Nick
- Dold, Christina
- Dong, Tao
- Pollard, Andrew J.
- Knight, Julian C.
- Klenerman, Paul
- Crook, Derrick
- Lambe, Teresa
- Clutterbuck, Elizabeth
- Bibi, Sagida
- Flaxman, Amy
- Bittaye, Mustapha
- Gilbert, Sarah
- Hall, David R.
- Williams, Mark A.
- Paterson, Neil G.
- James, William
- Carroll, Miles W.
- Fry, Elizabeth E.
- Mongkolsapaya, Juthathip
- Ren, Jingshan
- Stuart, David I.
- Screaton, Gavin R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 184
- Issue
- 8
- Pages
- 2201-2211.e7
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC7891044
- OpenAlex
- W3129558828
- Cited by
- 460
- References
- 60
- Citations by year
- 2025: 15 · 2024: 24 · 2023: 60 · 2022: 171 · 2021: 188 · 2020: 1
- FWCI
- 35.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Greater South Information System
- Funders
- UK Research and Innovation
- MRC (MR/N00065X/1)
- China Academy of Chinese Medical Sciences (2018-I2M-2-002)
- National Institute for Health Research (203141/Z/16/Z, 095541/A/11/Z, 090532/Z/09/Z)
- Coalition for Epidemic Preparedness Innovations
- Department of Health and Social Care
- NIHR Oxford Biomedical Research Centre
- National Institutes of Health (U19 I082360, WT204969/Z/16/Z)
- Wellcome Trust (101122/Z/13/Z)
- Cancer Research UK (C375/A17721)
- Chinese Academy of Medical Sciences
- Public Health England
- 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, B.1.1.7 variant, N501Y mutation, spike protein, antibody neutralization, antibody escape, monoclonal antibodies, convalescent sera, ACE2 binding
- MeSH terms
- COVID-19, SARS-CoV-2, Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Cricetulus, Humans, Protein Binding, Structure-Activity Relationship, Vero Cells, CHO Cells, Antibodies, Neutralizing, HEK293 Cells, Pandemics, Spike Glycoprotein, Coronavirus
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Claims read by deepseek-v4.1-flash under definition version 3 (extract-v3) on 2026-10-06.
Classified by jev-1.13-20260917 (gold-guideline-v0.2) on 2026-10-06.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review