SARS_CoV_2 mutation literature information.


  Impact of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Variant-Associated Receptor Binding Domain (RBD) Mutations on the Susceptibility to Serum Antibodies Elicited by Coronavirus Disease 2019 (COVID-19) Infection or Vaccination.
 PMID: 34309648       2022       Clinical infectious diseases
Abstract: RBD with E484K or E484Q mutation, either alone or in combination with other mutations, showed greatest reduction in serum IgG binding.


  In vitro data suggest that Indian delta variant B.1.617 of SARS-CoV-2 escapes neutralization by both receptor affinity and immune evasion.
 PMID: 34453338       2022       Allergy
Result: Anti-RBD IgG ELISA shows that antibodies induced by infection with wild-type Wuhan SARS-CoV-2 fail to recognize the RBD mutants L452R/E484Q (variant B.1.617) and E484K (variants P.1 and B.1.351), while recognition of RBDN440K is unaltered.
Result: As shown previously, vaccination induces antibodies with broader specificity than viral infection, resulting in antibodies that showed reduced binding to RBD carrying mutation E484K while all other RBDs, including the Indian variants of concern were recognized well by the vaccine-induced immune sera (Figure 3C).
Result: Binding kinetics of RBD mutants to ACE2 show increased af


  Post-Vaccination Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Infections and Incidence of the Presumptive B.1.427/B.1.429 Variant Among Healthcare Personnel at a Northern California Academic Medical Center.
 PMID: 34137815       2022       Clinical infectious diseases
Abstract: Available specimens were tested for L452R, N501Y, and E484K mutations using reverse-transcription polymerase chain reaction.


  An Update on Severe Acute Respiratory Syndrome Coronavirus 2 Diversity in the US National Capital Region: Evolution of Novel and Variants of Concern.
 PMID: 34272947       2022       Clinical infectious diseases
Abstract: A significant increase in t
Discussion: A regional variant was detected with increased prevalence in February 2021 that combined S: P681H and S: E484K.
Discussion: Notably, the circulation of variants carrying S: E484K has been temporary and the prevalence of this change remains sparse.


  Molecular definition of severe acute respiratory syndrome coronavirus 2 receptor-binding domain mutations: Receptor affinity versus neutralization of receptor interaction.
 PMID: 34240429       2022       Allergy
Abstract: In contrast, single mutation E484K had almost no impact on the binding kinetics, but essentially abolished recognition of RBD by convalescent sera.
Abstract: Interestingly, combining mutations E484K, K417N, and N501Y resulted in a RBD with both features: enhanced receptor binding and abolished immune recognition.
Abstract: METHODS: We produced wild type RBD, RBD with single mutations (E484K, K417N, or N501Y) or with all three mutations combined and tested their binding to ACE2 by biolayer interferometry (BLI).


  Spike protein cleavage-activation mediated by the SARS-CoV-2 P681R mutation: a case-study from its first appearance in variant of interest (VOI) A.23.1 identified in Uganda.
 PMID: 34230931       2022       bioRxiv
Abstract: The A.23 viral lineage, characterized by three spike mutations F157L, V367F and Q613H, was first identified in COVID-19 cases from a Ugandan prison in July 2020, and then was identified in the general population with additional spike mutations (
Introduction: This lineage then spilled into the general population adding additional spike mutations (R102I, L141F, E484K and P681R, as well as in nsp6, ORF8 and ORF9:to comprise lineage A.23.1:by September 2020.


  LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants.
 PMID: 33972947       2022       bioRxiv
Abstract: In pseudovirus neutralization studies, LY-CoV1404 retains potent neutralizing activity against numerous variants including B.1.1.7, B.1.351, B.1.617.2, B.1.427/B.1.429, P.1, B.1.526, B.1.1.529, and the BA.2 subvariant and retains binding to spike proteins with a variety of underlying RBD mutations including K417N, L452R, E484K, and N501Y.


  Antigenicity of the Mu (B.1.621) and A.2.5 SARS-CoV-2 Spikes.
 PMID: 35062348       2022       Viruses
Abstract: Some of the pivotal mutations such as N501Y and E484K in the receptor-binding domain (RBD) detected in B.1.1.7 (Alpha), B.1.351 (Beta) and P.1 (Gamma) are now present within the Mu variant.
Introduction: The Spike of Mu accumulated the following mutations: insertion in 146N, T95I, Y144T and Y145S, in the N-terminal domain (NTD); R346K, E484K, N501Y in the receptor-binding domain (RBD) and P681H at the S1/S2 interface.


  Efficacy of mRNA, adenoviral vector, and perfusion protein COVID-19 vaccines.
 PMID: 34906769       2022       Biomedicine & pharmacotherapy
Introduction: In the spike protein of the B.1.1.28 strain, there are eleven mutations, including L18F, T20N, P26S, D138Y, R190S, H655Y, T1027I, D614G, K417T, E484K, and N501Y.
Introduction: Strain B.1.351 contains nine mutations within spike protein, including the L18F, D80A, D215G, R246I, K417N, E484K,  PMID: 34909634       2022       Clinical infection in practice
Discussion: The E484Q mutation in the RBD, not present in the original B.1.628 isolate, is also present in the kappa variant of interest and thought to confer immune evasion similar to E484K, which alone reduced neutralizing titers by a median of 2.8-fold among recipients of mRNA vaccines for COVID-19.



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