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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.
Checked 2026-10-06 · 2 references not checked yet
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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.
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A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“As expected, there is little effect on many potent antibodies, for instance, the IGVH1-58 antibodies: 55, 165, 253, and 318.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
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In the paper
“the common IGLV1-9 antibodies (mAbs 150 and 158) show a consistent reduction in affinity of roughly 3-fold (Figure 3A).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
Strength:plain· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In contrast, mAb 222, which pairs IGHV3-53 with IGLV3-20, shows no reduction.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
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In the paper
“For the Pfizer-BioNTech vaccine BNT162b2, the reduction was 3.3-fold (geometric mean, n = 25 p < 0.0001) (Figure 5C).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Neutralization activity of convalescent plasma and vaccine sera
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Mass spectrometry and biolayer interferometry data confirmed the presence of tyrosine at 501.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Method details
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In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
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In the paper
“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)”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > The B.1.1.7 lineage
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Only a modest effect was observed with these antibodies (Figure 2C).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesA result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > The B.1.1.7 lineage
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- Probably not a substantial claim. 24
- It may state two separate claims as one. 24
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Electron density for the side chain of Y501 is weak.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Method details
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In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect of B.1.1.7 mutations on neutralization by potent mAbs
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In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Method details
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In the paper
“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%.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect of B.1.1.7 mutations on neutralization by potent mAbs
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In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on ACE2 affinity
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In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Method details
Strength:boosted· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
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In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > The B.1.1.7 lineage
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In the paper
“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”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
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In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
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In the paper
“During the week of December 24, 2020, the N501Y variant represented 53% of the sequenced isolates in Great Britain.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > The B.1.1.7 lineage
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The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Introduction
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In the paper
“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)”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Introduction
What the sources say
- Not checked yetcites Walker et al., 2021
Strength:hedged· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
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In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
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In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Neutralization activity of convalescent plasma and vaccine sera
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A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
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A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
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In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
What the sources say
- Not checked yetcites Zahradník et al., 2021
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“This construct encodes exactly the same protein as native RBD except the N501Y mutation, as confirmed by sequencing.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Method details
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A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
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In the paper
“As expected, there was a correlation between ACE2 blocking and neutralization titers”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
What the sources say
- Not checked yetcites Dejnirattisai et al., 2021 source
Strength:plain· not yet calibratedCausal:correlational· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
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In the paper
“An independent DSMB reviewed all interim safety reports.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
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A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Introduction
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None of the sources cited for this claim have been checked yet.
In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
What the sources say
- Not checked yetcites Sariol and Perlman, 2020
- Not checked yetcites Altmann and Boyton, 2020
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
In the paper
“indeed partial or non-neutralizing antibodies may confer protection (Henry Dunand et al., 2016).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
What the sources say
- Not checked yetcites Henry Dunand et al., 2016 source
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
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In the paper
“Written informed consent was obtained for all patients enrolled in the study.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
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A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“This alone might account for the selection of the N501Y mutation and an increase in transmission.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on ACE2 affinity
Tests✓ Asserted: passes✓ Checkable: passes✓ Load-bearing: passes✓ Based: passesIt may state two separate claims as one.
- 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.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
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In the paper
“These studies were registered at ISRCTN (15281137 and 89951424) and ClinicalTrials.gov (NCT04324606 and NCT04400838).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
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What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion > Limitations of the study
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✗ Based: failsProbably not a substantial claim. The paper’s conclusions may not depend on it. The paper may give no reason why it holds. It may state two separate claims as one.
In the paper
“It is believed that these mutations in the ACE2 receptor binding domain increase the affinity for ACE2 (Zahradník et al., 2021).”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Introduction
What the sources say
- Not checked yetcites Zahradník et al., 2021
Strength:hedged· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“Error bars are derived from curve fitting and may underestimate experimental error.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Results > Effect on mAb affinity
Strength:hedged· not yet calibratedCausal:conditional· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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].”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“The correlates of protection from SARS-CoV-2 infection are yet to be established.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion > Limitations of the study
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✗ Based: failsProbably not a substantial claim. The paper’s conclusions may not depend on it. The paper may give no reason why it holds.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > STAR★Methods > Experimental model and subject details
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion > Limitations of the study
Strength:plain· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes✗ Load-bearing: fails✓ Based: passesProbably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“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.”
§ Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera > Discussion
What the sources say
- Not checked yetcites Dejnirattisai et al., 2021 source
Strength:hedged· not yet calibratedCausal:direct· not yet calibratedTests✓ Asserted: passes✓ Checkable: passes? Load-bearing: unclear✓ Based: passesIt may state two separate claims as one.
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?
In the citing paper
“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]
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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.”
In the citing paper
“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]
In the citing paper
“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 the citing paper
“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]
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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.”
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Research works printed but not linked: 2
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- Zhu, 2021, Cryo-EM Structure of the N501Y SARS-CoV-2 Spike Protein in Complex with a Potent Neutralizing Antibody, bioRxiv
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“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].”
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Metadata
- 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
- 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
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