The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index; none of the 19 sources its claims cite is checked for support yet.
Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7
Open accessPublished version of a preprint
Abstract
The COVID-19 pandemic has had widespread effects across the globe, and its causative agent, SARS-CoV-2, continues to spread. Effective interventions need to be developed to end this pandemic. Single and combination therapies with monoclonal antibodies have received emergency use authorization 1-3, and more treatments are under development 4-7. Furthermore, multiple vaccine constructs have shown promise 8, including two that have an approximately 95% protective efficacy against COVID-19 9,10. However, these interventions were directed against the initial SARS-CoV-2 virus that emerged in 2019. The recent detection of SARS-CoV-2 variants B.1.1.7 in the UK 11 and B.1.351 in South Africa 12 is of concern because of their purported ease of transmission and extensive mutations in the spike protein. Here we show that B.1.1.7 is refractory to neutralization by most monoclonal antibodies against the N-terminal domain of the spike protein and is relatively resistant to a few monoclonal antibodies against the receptor-binding domain. It is not more resistant to plasma from individuals who have recovered from COVID-19 or sera from individuals who have been vaccinated against SARS-CoV-2. The B.1.351 variant is not only refractory to neutralization by most monoclonal antibodies against the N-terminal domain but also by multiple individual monoclonal antibodies against the receptor-binding motif of the receptor-binding domain, which is mostly due to a mutation causing an E484K substitution. Moreover, compared to wild-type SARS-CoV-2, B.1.351 is markedly more resistant to neutralization by convalescent plasma (9.4-fold) and sera from individuals who have been vaccinated (10.3-12.4-fold). B.1.351 and emergent variants 13,14 with similar mutations in the spike protein present new challenges for monoclonal antibody therapies and threaten the protective efficacy of current vaccines.
Overview
Integrity signals
Registry
Cites
Statistics
Figures
Verification
Claims the paper makes
38 Own result · 11 Not checked yet · 11 Own method · 9 Own interpretation
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
“Here we show that B.1.1.7 is refractory to neutralization by most monoclonal antibodies against the N-terminal domain of the spike protein and is relatively resistant to a few monoclonal antibodies against the receptor-binding domain.”
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“351 is mediated by the E484K substitution; the complete loss of activity of 910-30 is mediated by the K417N substitution; and the marked reduction in activity of REGN10933 is mediated by K417N and E484K, as has previously been reported 28 .”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Monoclonal antibodies
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“Here we show that B.1.1.7 is refractory to neutralization by most monoclonal antibodies against the N-terminal domain of the spike protein and is relatively resistant to a few monoclonal antibodies against the receptor-binding domain.”
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“Both B.1.1.7 and B.1.351are markedly resistant to neutralization by antibodies 5-24 and 4-8 20 , as well as by 4A8 29 , all of which target the antigenic supersite in the NTD 18 (Fig. 2b).”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Monoclonal antibodies
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“For neutralization of B.1.351,however, the activities of 910-30, 2-15 20 , LY-CoV555 (bamlanivimab) 1,23 , C121 24 and REGN10933 (casirivimab) 2 are completely or markedly abolished.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Monoclonal antibodies
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“The B.1.351variant is not only refractory to neutralization by most monoclonal antibodies against the N-terminal domain but also by multiple individual monoclonal antibodies against the receptor-binding motif of the receptor-binding domain, which is mostly due to a mutation causing an E484K”
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“We found that the resistance of B.1.1.7 to most NTD-directed monoclonal antibodies is largely conferred by ΔY144, whereas the resistance of B.1.351 is largely conferred by Δ242-Δ244 and/or R246I.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Monoclonal antibodies
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“The activity of CB6 is rendered inactive against B.1.351because of the K417N substitution.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Extended Data
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“Moreover, compared to wild-type SARS-CoV-2, B.1.351 is markedly more resistant to neutralization by convalescent plasma (9.4-fold) and sera from individuals who have been vaccinated (10.3-12.4-fold).”
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“We found that the resistance of B.1.1.7 to most NTD-directed monoclonal antibodies is largely conferred by ΔY144, whereas the resistance of B.1.351 is largely conferred by Δ242-Δ244 and/or R246I.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Monoclonal antibodies
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- It may state two separate claims as one. 12
- Probably not a substantial claim. 12
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
“Eight samples show a decrease of more than 2.5-fold in neutralizing activity against B.1.1.7Δ8,in contrast to the results for neutralization of B.1.1.7.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Convalescent plasma
plainn = 8- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
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
“Figure 3a shows that most (16 out of 20) plasma samples lost more than 2.5-fold neutralizing activity against B.1.351,while maintaining activity against B.1.1.7.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Convalescent plasma
plainn = 20- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
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
“Brii-196 and COV2-2130 are essentially unaffected by the new variants; the activities of Brii-198 and COV2-2196 are diminished by 14.6-fold and 6.3-fold, respectively, against B.1.351but not against B.1.1.7.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Extended Data
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
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
“Although S309 and the combination of Brii-196 and Brii-198 are not significantly impaired, their potencies are noticeably lower”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Extended Data
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
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
“Although REGN10933 and REGN10987 and COV2-2196 and COV2-2130 are seemingly unaffected against variant pseudoviruses, there are noticeable decreases in their activity against the B.1.351authentic virus.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Extended Data
hedgeddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“B.1.351and emergent variants 13,14 with similar mutations in the spike protein present new challenges for monoclonal antibody therapies and threaten the protective efficacy of current vaccines.”
What the sources say
- Not checked yetcites [13] Faria, N. R. et al. Genomic characterisation of an emergent SARS-CoV-2 lineage in Manaus: preliminary findings. Preprint at https://virological.org/t/genomic-characterisation-of-an-emergent-sars-cov-2-lineage-in-manaus-preliminary-findings/586 (2021).
- Not checked yetcites [14] Naveca, F. et al. Phylogenetic relationship of SARS-CoV-2 sequences from Amazonas with emerging Brazilian variants harboring mutations E484K and N501Y in the spike protein. Preprint at https://virological.org/t/phylogenetic-relationship-of-sars-cov-2-sequences-from-amazonas-with-emerging-brazilian-variants-harboring-mutations-e484k-and-n501y-in-the-spike-protein/585 (2021).
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Rests on an assumption: In vitro neutralization by monoclonal antibodies predicts clinical therapeutic efficacy.
- Rests on an assumption: In vitro neutralization by vaccinee sera predicts vaccine protective efficacy.
In the paper
“These discrepant results highlight a previous observation 20 that pseudovirus neutralization does not always faithfully”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Convalescent plasma
What the sources say
- Not checked yetcites [20] Liu, L. et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. Nature 584, 450–456 (2020). source
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim.
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
“All cell lines were obtained from authenticated vendors.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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 study protocol was approved by the CUIMC Institutional Review Board (IRB) and all participants provided written informed consent.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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
“No statistical methods were used to predetermine sample size.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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
“Viability was measured and found to be >90%.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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 experiments were not randomized and the investigators were not blinded to allocation during experiments and outcome assessment.”
- Also stated in: § Additional information · plain
“Randomization is not relevant as this is an observational study.”
- Also stated in: § Additional information · plain
“The investigators were not blinded as this is an observational study.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
- Also stated in: § Additional information · plain
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
“If the rampant spread of the virus continues and more critical mutations accumulate, then we may be condemned to chasing after the evolving SARS-CoV-2 continually, as we have long done for influenza virus.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Discussion
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: fails — It may be too vague to check against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may be too vague to check against evidence. 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
“Mycoplasma is negative (Detected mycoplasma contamination using Mycoplasma PCR ELISA ,Sigma,catalog number is 11663925910)”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“As for the ramifications of our findings for the protective efficacy of current SARS-CoV-2 vaccines, the neutralizing activity of sera from vaccinated individuals against B.1.1.7 is largely intact and no adverse effects on current vaccines are expected (Fig. 4c), consistent with conclusions that were reached by other studies 34,40,41 .”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Discussion
What the sources say
- Not checked yetcites [34] Wu, K. et al. mRNA-1273 vaccine induces neutralizing antibodies against spike mutants from global SARS-CoV-2 variants. Preprint at https://doi.org/10.1101/2021.01.25.427948 (2021). source
- Not checked yetcites [40] Collier, D. et al. SARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies. Preprint at https://doi.org/10.1101/2021.01.19.21249840 (2021). source
- Not checked yetcites [41] Muik, A. et al. Neutralization of SARS-CoV-2 lineage B.1.1.7 pseudovirus by BNT162b2 vaccine-elicited human sera. Science https://doi.org/10.1126/science.abg6105 (2021). source
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Rests on an assumption: In vitro neutralization by vaccinee sera predicts vaccine protective efficacy.
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
“Studies that were repeated are noted in figure captions and include all studies that demonstrated the key results reported in the manuscript.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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
“No data were excluded from the analysis”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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
“E484K causes not only steric clashes but also a charge change at antibody-binding sites, and thus abolishes binding by these RBM-directed monoclonal antibodies.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Extended Data
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
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
“Cytopathogenic effects of viral infection were visually scored for each well in a blinded manner by two independent observers.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably 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 sample size is appropriate within technical capability to compare the difference between groups”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Additional information
plain- Asserted: passes — The authors put it forward as true.
- Checkable: fails — It may be too vague to check against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: fails — The paper may give no reason why it holds.
Probably not a substantial claim. It may be too vague to check against evidence. The paper’s conclusions may not depend on it. The paper may give no reason why it holds.
None of the sources cited for this claim have been checked yet.
In the paper
“A total of 18 mutant pseudoviruses were made as previously described 20,21 , and each was found to have a robust titre (Extended Data Fig. 1c) that was adequate for neutralization studies.”
§ Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7 > Nature | Vol 593 | 6 May 2021 | 131
What the sources say
- Not checked yetcites [20] Liu, L. et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike. Nature 584, 450–456 (2020). source
- Not checked yetcites [21] Wang, P. et al. SARS-CoV-2 neutralizing antibody responses are more robust in patients with severe disease. Emerg. Microbes Infect. 9, 2091–2093 (2020). source
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
The paper relies on this without support.
In vitro neutralization by monoclonal antibodies predicts clinical therapeutic efficacy.
“These findings suggest that antibody treatment of this virus might need to be modified in localities in which B.1.351and related variants 13,14 are prevalent”
“Decisions on the use of these monoclonal antibodies will depend heavily on the local prevalence of B.1.351or variants with an E484K substitution”
The paper relies on this without support.
In vitro neutralization by vaccinee sera predicts vaccine protective efficacy.
“the neutralizing activity of sera from vaccinated individuals against B.1.1.7 is largely intact and no adverse effects on current vaccines are expected”
“threaten the protective efficacy of current vaccines”
The paper relies on this without support.
Reduced neutralization of a variant by antibodies in vitro reflects reduced antibody-mediated protection against that variant in vivo.
“Overall, the neutralizing activity against B.1.1.7 was essentially unchanged, but significantly lower against B.1.351(12.4-fold for the Moderna vaccine; 10.3-fold for the Pfizer vaccine).”
The paper relies on this without support.
The convalescent plasma samples and vaccinee sera studied are representative of convalescent patients and of vaccine recipients generally.
“B.1.351 is more resistant to neutralization by convalescent plasma from patients.”
“B.1.351 is more resistant to neutralization by sera from individuals vaccinated with the Moderna or Pfizer vaccine.”
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“E484K has resulted in 3-fold to 10-fold reduced susceptibility to about 30% and >10-fold reduced susceptibility to about 10% of convalescent plasma samples”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [121]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Some amino acid changes [Δ69/70, T95I, G142D, Δ145, K417N, T478K, N501Y, and P681H (T, Thr; I, Ile; G, Gly; D, Asp; K, Lys; N, Asn; Y, Tyr; P, Pro; H, His)] are shared mutations also found in the Alpha, Beta (B.1.351), Gamma (P.1), or Delta VOCs and were described to lead to increased transmissibility, as well as to a typically mild partial escape from vaccine-induced humoral immunity (7–10).”
From Neutralization of SARS-CoV-2 Omicron by BNT162b2 mRNA vaccine–elicited human sera (2022) · cites this paper as [7]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“As previously reported, bamlanivimab and etesivimab did not neutralize the Beta variant 21 .”
From Reduced sensitivity of SARS-CoV-2 variant Delta to antibody neutralization (2021) · cites this paper as [21]
In the citing paper
“Several of the RBD mutations directly affect angiotensin-converting enzyme 2 (ACE2) receptor-binding affinity, which may affect infectivity, viral load, or transmissibility.11, 12, 13, 14”
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 [14]
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 Wang et al., 2021
In the citing paper
“The Moderna mRNA-1273 vaccine also induces neutralizing antibodies to SARS-CoV-2 variants with, however, a five-to ten-fold reduction in efficacy against the B.1.351S protein, when compared to pseudovirus bearing the D614G mutation 27,28 .”
From Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies (2021) · cites this paper as [27]
In the citing paper
“The Pfizer Cominarty (also termed BNT162b2) vaccine-elicited human sera neutralizes SARS-CoV-2 lineage B.1.1.7 pseudovirus, with slightly reduced titers in some vaccinees, when compared to the Wuhan reference strain 26,27 .”
From Sensitivity of infectious SARS-CoV-2 B.1.1.7 and B.1.351 variants to neutralizing antibodies (2021) · cites this paper as [27]
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 [121]
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 [121]
In the citing paper
“The Beta variant is associated with reduced susceptibility to many mAbs because E484K interferes with binding of several RBM class 1 and 2 mAbs and K417N interferes with the binding of several RBM class 1 mAbs 104,117,121,163,217 .”
From The biological and clinical significance of emerging SARS-CoV-2 variants (2021) · cites this paper as [121]
In the citing paper
“In multiple studies, B.1.351 was the most resistant to neutralization by convalescent or vaccinee sera, with 6- to 15-fold less neutralization activity for sera from individuals immunized with vaccines based on the virus strain first described in January 2020 (Wuhan-Hu-1, spike also called WA1) (2–9).”
From Durability of mRNA-1273 vaccine–induced antibodies against SARS-CoV-2 variants (2021) · cites this paper as [5]
In the citing paper
“Most of these prior studies have evaluated sera from vaccinated individuals at time points soon after the first or second dose and have had limited data on the durability of such responses.”
From Durability of mRNA-1273 vaccine–induced antibodies against SARS-CoV-2 variants (2021) · cites this paper as [5]
In the citing paper
“However, reduced sensitivity of SARS-CoV-2 variants to antibody and serum neutralization has been widely observed (18–21).”
From Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization (2022) · cites this paper as [21]
In the citing paper
“Beta [as a benchmark for partially reduced neutralization (7) without major impact on effectiveness (19, 20)]”
From Neutralization of SARS-CoV-2 Omicron by BNT162b2 mRNA vaccine–elicited human sera (2022) · cites this paper as [7]
In the citing paper
“Several SARS-CoV-2 variants of concern have emerged that display increased transmissibility or reduced in-vitro neutralisation by sera from people who are infected with the ancestral strain or immunised.2, 3, 4”
From Neutralising antibody titres as predictors of protection against SARS-CoV-2 variants and the impact of boosting: a meta-analysis (2022) · cites this paper as [2]
Citations
Cites
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
Korber, B., Fischer, W. M., Gnanakaran, S., Yoon, H., Theiler, J., Abfalterer, W., Hengartner, N., Giorgi, E. E., Bhattacharya, T., Foley, B., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.043 · Cited by 4,281
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2020) · doi:10.1101/2020.12.21.20248640 · Cited by 2,535
Detection of a SARS-CoV-2 variant of concern in South Africa
Tegally, H., Wilkinson, E., Giovanetti, M., Iranzadeh, A., Fonseca, V., Giandhari, J., Doolabh, D., Pillay, S., San, E. J., Msomi, N., et al. (2021) · Nature · doi:10.1038/s41586-021-03402-9 · Cited by 2,510
SARS-CoV-2 vaccines in development
Krammer, F. (2020) · Nature · doi:10.1038/s41586-020-2798-3 · Cited by 2,098
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
Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
Pinto, D., Park, Y.-J., Beltramello, M., Walls, A. C., Tortorici, M. A., Bianchi, S., Jaconi, S., Culap, K., Zatta, F., De Marco, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2349-y · Cited by 1,885
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853
Human neutralizing antibodies elicited by SARS-CoV-2 infection
Ju, B., Zhang, Q., Ge, J., Wang, R., Sun, J., Ge, X., Yu, J., Shan, S., Zhou, B., Song, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2380-z · Cited by 1,667
Self-citationSafety and Immunogenicity of SARS-CoV-2 mRNA-1273 Vaccine in Older Adults
Anderson, E. J., Rouphael, N. G., Widge, A. T., Jackson, L. A., Roberts, P. C., Makhene, M., Chappell, J. D., Denison, M. R., Stevens, L. J., Pruijssers, A. J., et al. (2020) · New England Journal of Medicine · doi:10.1056/nejmoa2028436 · Cited by 1,523
Self-citation
Research works printed but not linked: 2
- Faria, N. R. et al. Genomic characterisation of an emergent SARS-CoV-2 lineage in Manaus: preliminary findings. Preprint at https://virological.org/t/genomic-characterisation-of-an-emergent-sars-cov-2-lineage-in-manaus-preliminary-findings/586 (2021).
- Naveca, F. et al. Phylogenetic relationship of SARS-CoV-2 sequences from Amazonas with emerging Brazilian variants harboring mutations E484K and N501Y in the spike protein. Preprint at https://virological.org/t/phylogenetic-relationship-of-sars-cov-2-sequences-from-amazonas-with-emerging-brazilian-variants-harboring-mutations-e484k-and-n501y-in-the-spike-protein/585 (2021).
Cited by
Sorted by citations
Items 701–800 of 1,015
Perlin, D. S., Neil, G. A., Anderson, C. S., Zafir‐Lavie, I., Raines, S. R., Ware, C. F., & Wilkins, H. J. (2021) · Journal of Clinical Investigation · doi:10.1172/jci153173 · Cited by 32
Nesterenko, P. A., McLaughlin, J., Tsai, B. L., Sojo, G. B., Cheng, D., Zhao, D. Y., Mao, Z., Bangayan, N. J., Obusan, M. B., Su, Y., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110167 · Cited by 33
Wang, Y.-D., Liu, M., Shen, Y., Ma, Y., Li, X., Zhang, Y., Liu, M., Yang, X., Chen, J., Yan, R., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00401-6 · Cited by 32
Next-Generation Serology by Mass Spectrometry: Readout of the SARS-CoV-2 Antibody Repertoire
Melani, R. D., Soye, B. J. D., Kafader, J. O., Forte, E., Hollas, M. A. R., Blagojevic, V., Negrão, F., McGee, J. P., Drown, B., Lloyd-Jones, C., et al. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.1c00882 · Cited by 32
Mirahmadizadeh, A., Heiran, A., Lankarani, K. B., Serati, M., Habibi, M., Eilami, O., Heiran, F., & Moghadami, M. (2022) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofac177 · Cited by 32
Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529
Wang, Q., Anang, S., Iketani, S., Guo, Y., Liu, L., Katsamba, P. S., Shapiro, L. S., Ho, D. D., & Sodroski, J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110924 · Cited by 34
Self-citationBates, T. A., Lu, P., Kang, Y. J., Schoen, D., Thornton, M. A., McBride, S. K., Park, C., Kim, D., Messer, W. B., Curlin, M. E., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111544 · Cited by 32
An overview of viral mutagenesis and the impact on pathogenesis of SARS-CoV-2 variants
Khan, M. Z. I., Nazli, A., Al-furas, H., Asad, M. I., Ajmal, I., Khan, D., Shah, J., Farooq, M. A., & Jiang, W. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1034444 · Cited by 37
Effectiveness of COVID‑19 vaccines and their challenges (Review)
Marfè, G., Perna, S., & Shukla, A. K. (2021) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2021.10843 · Cited by 32
Structural understanding of SARS-CoV-2 virus entry to host cells
Le, K. P. U., Kannappan, S., Kim, T., Lee, J. H., Lee, H.-R., & Kim, K. K. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1288686 · Cited by 34
Rao, X., Zhao, R., Tong, Z., Guo, S., Peng, W., Liu, K., Li, S., Wu, L., Tong, J., Chai, Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314193120 · Cited by 31
An update on the anti-spike monoclonal antibody pipeline for SARS-CoV-2
Focosi, D., Franchini, M., Casadevall, A., & Maggi, F. (2024) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2024.04.012 · Cited by 31
Mutational dynamics of SARS-CoV-2: Impact on future COVID-19 vaccine strategies
Faraji, N., Zeinali, T., Joukar, F., Aleali, M. S., Eslami, N., Shenagari, M., & Mansour‐Ghanaei, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e30208 · Cited by 32
Zhou, X., Ma, F., Xie, J., Yuan, M., Li, Y., Shaabani, N., Zhao, F., Huang, D., Wu, N. C., Lee, C.-C. D., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109109 · Cited by 31
Tostanoski, L. H., Yu, J., Mercado, N. B., McMahan, K., Jacob-Dolan, C., Martinot, A. J., Piedra-Mora, C., Anioke, T., Chang, A., Giffin, V. M., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abj3789 · Cited by 31
Self-citationA bivalent nanoparticle vaccine exhibits potent cross-protection against the variants of SARS-CoV-2
Yuan, Y., Zhang, X., Chen, R., Li, Y., Wu, B., Li, R., Zou, F., Ma, X., Wang, X., Chen, Q., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110256 · Cited by 31
Targeted vaccination and the speed of SARS-CoV-2 adaptation
Gandon, S., & Lion, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2110666119 · Cited by 33
Co-circulation of SARS-CoV-2 Alpha and Gamma variants in Italy, February and March 2021
Stefanelli, P., Trentini, F., Dirani, G., Marziano, V., Mammone, A., Poletti, P., Grané, C. M., Manica, M., Manso, M. D., Andrianou, X. D., et al. (2022) · Eurosurveillance · doi:10.2807/1560-7917.es.2022.27.5.2100429 · Cited by 32
Chen, R., Zhang, X., Yuan, Y., Deng, X., Wu, B., Xi, Z., Wang, G., Lin, Y., Li, R., Wang, X., et al. (2022) · Advanced Science · doi:10.1002/advs.202105378 · Cited by 31
Xu, K., Fan, C., Han, Y., Dai, L., & Gao, G. F. (2022) · International Immunology · doi:10.1093/intimm/dxac031 · Cited by 31
Liu, H., Kaku, C. I., Song, G., Yuan, M., Andrabi, R., Burton, D. R., Walker, L. M., & Wilson, I. A. (2022) · Communications Biology · doi:10.1038/s42003-022-03700-6 · Cited by 32
Dicken, S. J., Murray, M. J., Thorne, L., Reuschl, A., Forrest, C., Ganeshalingham, M., Muir, L., Kalemera, M. D., Palor, M., McCoy, L. E., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.22.436468 · Cited by 30
The SARS-CoV-2 Delta variant is poised to acquire complete resistance to wild-type spike vaccinesPreprint
Liu, Y., Arase, N., Kishikawa, J.-I., Hirose, M., Li, S., Tada, A., Matsuoka, S., Arakawa, A., Akamatsu, K., Ono, C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.08.22.457114 · Cited by 31
Chen, Y., Yang, W., Chen, H., Huang, L., Gao, J.-Y., Lin, C., Wang, Y.-C., Yang, C., Liu, Y., Hou, M., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101658 · Cited by 30
Neerukonda, S. N., Vassell, R. A., Lusvarghi, S., Wang, R., Echegaray, F., Bentley, L., Eakin, A. E., Erlandson, K. J., Katzelnick, L. C., Weiss, C. D., et al. (2021) · Viruses · doi:10.3390/v13122485 · Cited by 31
Virus Infection and Systemic Inflammation: Lessons Learnt from COVID-19 and Beyond
Faist, A., Janowski, J., Kumar, S., Hinse, S., Çalışkan, D. M., Lange, J., Ludwig, S., & Brunotte, L. (2022) · Cells · doi:10.3390/cells11142198 · Cited by 31
Zhao, X., Qiu, T., Huang, X., Mao, Q., Wang, Y., Qiao, R., Li, J., Mao, T., Wang, Y., Cun, Y., et al. (2024) · Cell Discovery · doi:10.1038/s41421-024-00648-1 · Cited by 30
Self-citationIssa, H., Eid, A. H., Berry, B., Takhviji, V., Khosravi, A., Mantash, S., Nehme, R., Hallal, R., Karaki, H., Dhayni, K., et al. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.620990 · Cited by 30
Pandemic moves and countermoves: vaccines and viral variants
Sanders, R. W., & de Jong, M. D. (2021) · The Lancet · doi:10.1016/s0140-6736(21)00730-3 · Cited by 33
Miao, M., Clercq, E. D., & Li, G. (2021) · Biomedicines · doi:10.3390/biomedicines9040412 · Cited by 32
Inhibitory effect on SARS‐CoV‐2 infection of neferine by blocking Ca2+‐dependent membrane fusion
Yang, Y., Yang, P., Huang, C., Wu, Y., Zhou, Z., Wang, X., & Wang, S. (2021) · Journal of Medical Virology · doi:10.1002/jmv.27117 · Cited by 30
Li, X., Zhang, L., Chen, S. E., Ji, W., Li, C., & Ren, L. (2021) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2021.104971 · Cited by 30
Stankov, M. V., Cossmann, A., Bonifacius, A., Dopfer‐Jablonka, A., Ramos, G. M., Gödecke, N., Scharff, A. Z., Happle, C., Boeck, A.-L., Tran, A. T., et al. (2021) · Clinical Infectious Diseases · doi:10.1093/cid/ciab555 · Cited by 31
Olsen, R. J., Christensen, P. A., Long, S. W., Subedi, S., Hodjat, P., Olson, R., Nguyen, M., Davis, J. J., Yerramilli, P., Saavedra, M. O., et al. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.07.002 · Cited by 30
Rainwater‐Lovett, K., Redd, J. T., Stewart, M. A., Calles, N. E., Cluff, T., Fang, M., Panaggio, M. J., Lambrou, A. S., Thornhill, J., Bradburne, C. E., et al. (2021) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofab398 · Cited by 30
Genomic surveillance of SARS-CoV-2 Spike gene by sanger sequencing
Salles, T. S., Cavalcanti, A. C., da Costa, F. B., Dias, V. Z., de Souza, L. M., de Meneses, M. D. F., da Silva, J. A. S., Amaral, C. D., Felix, J. R., Pereira, D. A., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0262170 · Cited by 30
RBD trimer mRNA vaccine elicits broad and protective immune responses against SARS-CoV-2 variants
Liang, Q., Wang, Y., Zhang, S., Sun, J., Sun, W., Li, J., Liu, Y., Li, M., Cheng, L., Jiang, Y., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104043 · Cited by 31
Seki, Y., Yoshihara, Y., Nojima, K., Momose, H., Fukushi, S., Moriyama, S., Wagatsuma, A., Numata, N., Sasaki, K., Kuzuoka, T., et al. (2022) · Med · doi:10.1016/j.medj.2022.04.013 · Cited by 30
Wang, S., Sun, H., Zhang, Y., Yuan, L., Wang, Y., Zhang, T., Wang, S., Zhang, J., Yu, H. J., Xiong, H., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110862 · Cited by 30
Self-citationParzych, E. M., Du, J., Ali, A., Schultheis, K., Frase, D. M., Smith, T. R. F., Cui, J., Chokkalingam, N., Tursi, N. J., Andrade, V. M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33309-6 · Cited by 30
Ascertainment rate of SARS-CoV-2 infections from healthcare and community testing in the UK
Colman, E. R., Puspitarani, G. A., Enright, J. A., & Kao, R. R. (2022) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2022.111333 · Cited by 32
Li, L., Chen, X., Wang, Z., Li, Y., Wang, C., Jiang, L., & Zuo, T. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011856 · Cited by 30
Evaluation of two RT-PCR screening assays for identifying SARS-CoV-2 variants
Migueres, M., Lhomme, S., Trémeaux, P., Dimeglio, C., Ranger, N., Latour, J., Dubois, M., Nicot, F., Miédougé, M., Mansuy, J., et al. (2021) · Journal of Clinical Virology · doi:10.1016/j.jcv.2021.104969 · Cited by 30
Evolution of Antiviral Drug Resistance in SARS-CoV-2
Dinata, R., Baindara, P., & Mandal, S. M. (2025) · Viruses · doi:10.3390/v17050722 · Cited by 31
Nuñez, I. A., Lien, C. Z., Selvaraj, P., Stauft, C. B., Liu, S., Starost, M. F., & Wang, T. T. (2021) · mSphere · doi:10.1128/msphere.00507-21 · Cited by 29
SARS-CoV-2 mutations in Brazil: from genomics to putative clinical conditions
Timmers, L. F. S. M., Peixoto, J. V., Ducati, R. G., Bachega, J. F. R., Pereira, L. D. M., Caceres, R. A., Majolo, F., da Silva, G. L., Anton, D. B., Dellagostin, O. A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-91585-6 · Cited by 30
Nörz, D. S., Grunwald, M., Olearo, F., Fischer, N., Aepfelbacher, M., Pfefferle, S., & Lütgehetmann, M. (2021) · Journal of Clinical Virology · doi:10.1016/j.jcv.2021.104894 · Cited by 30
Anti-SARS-CoV-2 Vaccines and Monoclonal Antibodies Facing Viral Variants
Chaqroun, A., Hartard, C., & Schvoerer, É. (2021) · Viruses · doi:10.3390/v13061171 · Cited by 31
Tang, J., Lee, Y., Ravichandran, S., Grubbs, G., Huang, C., Stauft, C. B., Wang, T. T., Golding, B., Golding, H., & Khurana, S. (2021) · iScience · doi:10.1016/j.isci.2021.103006 · Cited by 29
Chen, H.-Y., Huang, C., Tian, L., Huang, X., Zhang, C., Llewellyn, G. N., Rogers, G. L., Andresen, K., O’Gorman, M. R. G., Chen, Y., et al. (2021) · Journal of Virology · doi:10.1128/jvi.00966-21 · Cited by 31
Yuan, T. Z., Garg, P., Wang, L., Willis, J. R., Kwan, E., Hernandez, A. G. L., Tuscano, E., Sever, E. N., Rivera, E. K., Soto, C. S., et al. (2021) · mAbs · doi:10.1080/19420862.2021.2002236 · Cited by 31
Salazar–García, M., Acosta-Contreras, S., Martinez, G. R., Cruz‐Rangel, A., Flores-Alanis, A., Patiño‐López, G., & Luna-Pineda, V. M. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.817200 · Cited by 29
Yuan, L., Zhou, M., Zhou, M., Ma, J., Chen, P., Liu, X., Wu, K., Cheng, T., Liu, Q., Hou, W., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00793-7 · Cited by 29
Rapid detection of multiple SARS-CoV-2 variants of concern by PAM-targeting mutations
Ning, B., Youngquist, B. M., Li, D. D., Lyon, C. J., Zelazny, A. M., Maness, N. J., Tian, D., & Hu, Y. (2022) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100173 · Cited by 29
Neutralizing Monoclonal Antibodies Inhibit SARS-CoV-2 Infection through Blocking Membrane Fusion
Li, C., Chao, T., Chang, T.-Y., Hsiao, C.-C., Lu, D.-C., Chiang, Y.-W., Lai, G.-C., Tsai, Y., Fang, J., Ieong, S., et al. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.01814-21 · Cited by 29
Research progress on vaccine efficacy against SARS-CoV-2 variants of concern
Bian, L., Liu, J., Gao, F., Gao, Q., He, Q., Mao, Q., Wu, X., Xu, M., & Liang, Z. (2022) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2022.2057161 · Cited by 30
El-Malah, S. S., Saththasivam, J., Jabbar, K. A., Arun, K. K., Gomez, T., Ahmed, A. A., Mohamoud, Y. A., Malek, J. A., Abu-Raddad, L. J., Halaweh, H. A. A., et al. (2022) · Environmental Technology & Innovation · doi:10.1016/j.eti.2022.102775 · Cited by 30
The Role of Cellular Immunity in the Protective Efficacy of the SARS-CoV-2 Vaccines
Sun, Z., Wu, T., Xie, H., Li, Y., Zhang, J., Su, X., & Qi, H. (2022) · Vaccines · doi:10.3390/vaccines10071103 · Cited by 29
Zhan, W., Tian, X., Zhang, X., Xing, S., Song, W., Liu, Q., Hao, A., Hu, Y., Zhang, M., Ying, T., et al. (2022) · Journal of Virology · doi:10.1128/jvi.00480-22 · Cited by 29
The Coming of Age of Nucleic Acid Vaccines during COVID-19
Rando, H. M., Lordan, R., Kolla, L., Sell, E., Lee, A. J., Wellhausen, N., Naik, A. S., Kamil, J. P., Gitter, A., Greene, C. S., et al. (2023) · mSystems · doi:10.1128/msystems.00928-22 · Cited by 30
Karges, J., Giardini, M. A., Blacque, O., Woodworth, B., Siqueira-Neto, J. L., & Cohen, S. M. (2022) · Chemical Science · doi:10.1039/d2sc05473f · Cited by 29
Kwon, P. S., Xu, S., Oh, H., Kwon, S., Rodrigues, A. L., Feroz, M. M., Fraser, K., He, P., Zhang, F., Hong, J. J., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04789-z · Cited by 30
Gorman, M. J., Patel, N., Guebre‐Xabier, M., Zhu, A. L., Atyeo, C. G., Pullen, K. M., Loos, C., Goez-Gazi, Y., Carrion, R., Tian, J.-H., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.05.429759 · Cited by 29
ChAdOx1 nCoV-19 (AZD1222) protects Syrian hamsters against SARS-CoV-2 B.1.351 and B.1.1.7Preprint
Fischer, R. J., van Doremalen, N., Adney, D. R., Yinda, C. K., Port, J. R., Holbrook, M. G., Schulz, J. E., Williamson, B. N., Thomas, T., Barbian, K., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.11.435000 · Cited by 29
Structure-activity relationships of B.1.617 and other SARS-CoV-2 spike variantsPreprint
Yang, T., Yu, P., Chang, Y., Chang, N.-E., Tsai, Y.-X., Liang, K.-H., Drączkowski, P., Lin, B., Wang, Y., Chien, Y.-C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.12.459978 · Cited by 30
Annals of Pharmacology and Pharmaceutics
States, U. (2020) · Annals of Pharmacology and Pharmaceutics · doi:10.25107/2573-6051 · Cited by 29
Ma, Y., Wu, H., Chen, S., Xie, C., Hu, J., Qi, X., Ma, X., Chu, Y., Shan, J., Lu, Y. Z., et al. (2023) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2023.115456 · Cited by 28
Structural Immunology of SARS ‐ CoV ‐2
Yuan, M., & Wilson, I. A. (2024) · Immunological Reviews · doi:10.1111/imr.13431 · Cited by 29
Meta-Analysis and Structural Dynamics of the Emergence of Genetic Variants of SARS-CoV-2
Castonguay, N., Zhang, W., & Langlois, M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.676314 · Cited by 28
The Emergence and Spread of Novel SARS-CoV-2 Variants
Yi, H., Wang, J., Wang, J., Lu, Y., Zhang, Y., Peng, R., Lu, J., & Chen, Z. (2021) · Frontiers in Public Health · doi:10.3389/fpubh.2021.696664 · Cited by 29
Siracusano, G., Brombin, C., Pastori, C., Cugnata, F., Noviello, M., Tassi, E., Princi, D., Cantoni, D. M., Malnati, M., Maugeri, N., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.772239 · Cited by 29
Mapping cross-variant neutralizing sites on the SARS-CoV-2 spike protein
Xu, S., Wang, Y., Wang, Y., Zhang, C., Qin, H., Gu, C., Xu, R., Wang, T., Yang, Y. P., Zang, J., et al. (2021) · Emerging Microbes & Infections · doi:10.1080/22221751.2021.2024455 · Cited by 28
Structural Comparison and Drug Screening of Spike Proteins of Ten SARS-CoV-2 Variants
Yang, Q., Jian, X., Syed, A. A. S., Fahira, A., Zheng, C., Zhu, Z., Wang, K., Zhang, J., Wen, Y., Li, Z., et al. (2022) · Research · doi:10.34133/2022/9781758 · Cited by 30
Therapeutic antibodies for COVID-19: is a new age of IgM, IgA and bispecific antibodies coming?
Zhang, J., Zhang, H., & Sun, L. (2022) · mAbs · doi:10.1080/19420862.2022.2031483 · Cited by 28
Basheer, A., & Zahoor, I. (2021) · Microorganisms · doi:10.3390/microorganisms9122609 · Cited by 28
Prajapati, J., Patel, R., Rao, P., Saraf, M. S., Rawal, R., & Goswami, D. (2022) · Structural Chemistry · doi:10.1007/s11224-022-01932-0 · Cited by 28
Design, immunogenicity, and efficacy of a pan-sarbecovirus dendritic-cell targeting vaccine
Coléon, S., Wiedemann, A., Surénaud, M., Lacabaratz, C., Hüe, S., Prague, M., Cervantes-Gonzalez, M., Wang, Z., Ellis, J., Sansoni, A., et al. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104062 · Cited by 29
SARS-CoV-2 Omicron Variants Reduce Antibody Neutralization and Acquire Usage of Mouse ACE2
Wang, R., Zhang, Q., Zhang, R., Aw, Z. Q., Chen, P., Wong, Y. H., Hong, J., Ju, B., Shi, X., Ding, Q., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.854952 · Cited by 29
Toledo-Romaní, M. E., Carmenate, M. G., Verdecia-Sánchez, L., Pérez-Rodríguez, S., Rodriguez-González, M., Valenzuela‐Silva, C., Paredes-Moreno, B., Sánchez-Ramírez, B., González-Mugica, R., Hernández-García, T., et al. (2022) · Med · doi:10.1016/j.medj.2022.08.001 · Cited by 30
Wu, J., Chen, Z., Gao, Y., Wang, Z., Wang, J., Chiang, B., Zhou, Y., Han, Y., Zhan, W., Xie, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112503 · Cited by 28
Nasiri, K., Mohammadzadehsaliani, S., Kheradjoo, H., Shabestari, A. M., Eshaghizadeh, P., Pakmehr, A., Alsaffar, M. F., Al-Naqeeb, B. Z. T., Yasamineh, S., & Gholizadeh, O. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01122-3 · Cited by 28
Broadly neutralizing antibodies to SARS-related viruses can be readily induced in rhesus macaques
He, W., Yuan, M., Callaghan, S., Musharrafieh, R. G., Song, G., Silva, M., Beutler, N., Lee, W.-H., Yong, P., Torres, J. L., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abl9605 · Cited by 32
Graham, C., Seow, J., Huettner, I., Khan, H., Kouphou, N., Acors, S., Winstone, H., Pickering, S., Galao, R. P., Lista, M. J., et al. (2021) · doi:10.1101/2021.02.03.429355 · Cited by 27
Sah, R., Khatiwada, A. P., Shrestha, S., Bhuvan, K. C., Tiwari, R., Mohapatra, R. K., Dhama, K., & Rodriguez-Morales, A. J. (2021) · Travel Medicine and Infectious Disease · doi:10.1016/j.tmaid.2021.102037 · Cited by 27
SARS-CoV-2 cell entry and targeted antiviral development
Chen, Z., Du, R., Achi, J. G., Rong, L., & Cui, Q. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.05.007 · Cited by 27
Monrad, I., Sahlertz, S. R., Nielsen, S. S. F., Pedersen, L. Ø., Petersen, M. S., Kobel, C. M., Tarpgaard, I. H., Storgaard, M., Mortensen, K. L., Schleimann, M. H., et al. (2021) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofab295 · Cited by 27
Adaptation of the endemic coronaviruses HCoV-OC43 and HCoV-229E to the human host
Forni, D., Cagliani, R., Arrigoni, F., Benvenuti, M., Mozzi, A., Pozzoli, U., Clerici, M., GIOIA, L. D., & Sironi, M. (2021) · Virus Evolution · doi:10.1093/ve/veab061 · Cited by 30
Beta RBD boost broadens antibody-mediated protection against SARS-CoV-2 variants in animal models
Sheward, D. J., Mandolesi, M., Urgard, E., Kim, C., Hanke, L., Vidakovics, L. P., Pankow, A. P., Smith, N. L., Dopico, X. C., McInerney, G. M., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100450 · Cited by 28
Biparatopic nanobodies protect mice from lethal challenge with SARS‐CoV‐2 variants of concern
Wagner, T. R., Schnepf, D., Beer, J., Klingel, K., Ruetalo, N., Kaiser, P. D., Junker, D., Sauter, M., Traenkle, B., Frecot, D. I., et al. (2021) · EMBO Reports · doi:10.15252/embr.202153865 · Cited by 27
van Gils, M. J., van Willigen, H. D. G., Wynberg, E., Han, A. X., van der Straten, K., Burger, J. A., Poniman, M., Oomen, M., Tejjani, K., Bouhuijs, J. H., et al. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100486 · Cited by 29
Dhawan, M. K., Priyanka, Parmar, M., Angural, S., & Choudhary, O. P. (2021) · International Journal of Surgery · doi:10.1016/j.ijsu.2021.106204 · Cited by 27
A review of the safety and efficacy of current COVID-19 vaccines
Huang, Z., Su, Y., Zhang, T., & Xia, N. (2022) · Frontiers of Medicine · doi:10.1007/s11684-021-0893-y · Cited by 28
Noor, R., Shareen, S., & Billah, M. (2022) · Bulletin of the National Research Centre/Bulletin of the National Research Center · doi:10.1186/s42269-022-00787-z · Cited by 29
Greaney, A. J., Eguia, R. T., Starr, T. N., Khan, K., Franko, N., Logue, J. K., Lord, S. M., Speake, C., Chu, H. Y., Sigal, A., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010592 · Cited by 29
Evolving antibody evasion and receptor affinity of the Omicron BA.2.75 sublineage of SARS-CoV-2
Wang, Q., Li, Z., Guo, Y., Mellis, I. A., Iketani, S., Liu, M., Yu, J., Valdez, R., Lauring, A. S., Sheng, Z., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108254 · Cited by 27
Self-citationOrtega, J. T., Pujol, F. H., Jastrzębska, B., & Rangel, H. R. (2021) · EXCLI journal · doi:10.17179/excli2021-3471 · Cited by 26
Initial experience of bamlanivimab monotherapy use in solid organ transplant recipients
Kutzler, H. L., Kuzaro, H. A., Serrano, O. K., Feingold, A. D., Morgan, G., & Cheema, F. (2021) · Transplant Infectious Disease · doi:10.1111/tid.13662 · Cited by 26
Cross-Reactive SARS-CoV-2 Neutralizing Antibodies From Deep Mining of Early Patient Responses
Bullen, G., Galson, J. D., Hall, G., Villar, P., Moreels, L., Ledsgaard, L., Mattiuzzo, G., Bentley, E. M., Masters, E. W., Tang, D. G., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.678570 · Cited by 26
Kaku, Y., Kuwata, T., Zahid, H. M., Hashiguchi, T., Noda, T., Kuramoto, N., Biswas, S., Matsumoto, K., Shimizu, M., Kawanami, Y., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109385 · Cited by 26
Liu, Z., Wu, H., Egland, K. A., Gilliland, T. C., Dunn, M. D., Luke, T. C., Sullivan, E. J., Klimstra, W. B., Bausch, C. L., & Whelan, S. P. J. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1940652 · Cited by 26
Metadata
- Authors
- Wang, P., Nair, M. S., Liu, L., Iketani, S., Luo, Y., Guo, Y., Wang, M., Yu, J., Zhang, B., Kwong, P. D., Graham, B. S., Mascola, J. R., Chang, J. Y., Yin, M. T., Sobieszczyk, M., Kyratsous, C. A., Shapiro, L., Sheng, Z., Huang, Y., & Ho, D. D.
- Affiliations
- Aaron Diamond AIDS Research Center (US)
- National Institutes of Health (US)
- Regeneron (United States) (US)
- Corresponding author
- Huang, Yaoxing
- Ho, David D.
- ORCID
- Venue
- Nature
- Published
- 2021-03-08
- Volume
- 593
- Issue
- 7857
- Pages
- 130-135
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7852232
- OpenAlex
- W3123551159
- Cited by
- 2,312
- References
- 51
- Citations by year
- 2026: 34 · 2025: 101 · 2024: 136 · 2023: 299 · 2022: 750 · 2021: 984
- FWCI
- 171.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Research Square (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, cc-by)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Bill and Melinda Gates Foundation
- JPB Foundation
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- SARS-CoV-2, SARS-CoV-2 variants, Beta variant, Alpha variant, antibody resistance, neutralizing antibodies, monoclonal antibodies, spike protein mutations, N-terminal domain, receptor binding domain, convalescent plasma, vaccine efficacy
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.
A language model drew the claims from the paper on 2026-10-06, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-06 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
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
