Discussion: Even the Delta variant, with only two mutations in the RBD (L452R and T478K) has significantly reduced antibody neutralisation effects, suggestive of how specific vaccine-derived antibodies can be.
Functional Analysis of Spike from SARS-CoV-2 Variants Reveals the Role of Distinct Mutations in Neutralization Potential and Viral Infectivity.
Discussion: N501Y L452R, E484K S477S, and T478K distinct RBD mutations potentially compromise the efficacy of administrated vaccines.
Discussion: However, RBD-specific mutations like N501Y, E484K, S477N, and L452R K417N, which lay within or close to the binding surface to ACE2, will keep playing key roles in respectively affecting binding of the spike to the receptor or escaping from mAb.
Discussion: Single L452R and T478K PMID: 35461042
2022
Journal of clinical virology
Discussion: BD-368-2 and C110 totally lost their binding activities to the RBD-L452R, but still maintained some degree of affinity to the RBD-L452Q, suggesting that an arginine at L452 residual might have a greater impact on antibody recognition than the glutamine.
Discussion: The more common mutation at L452 in the RBD was the L452R substitution, which has been found in Epsilon, Kappa, and Delta variants.
Discussion: Thus, we performed a head-to-head comparison of the binding affinity of nAbs to the RBD-L452R and RBD-L452Q.
Decreased and Heterogeneous Neutralizing Antibody Responses Against RBD of SARS-CoV-2 Variants After mRNA Vaccination.
Abstract: The most significant increase was observed in variants Epsilon and Delta, containing mutation L452R.
Method: Primers used for the construction of the RBD-mFc proteins for the different
Result: Consistent with previous studies, these results point to a substantial contribution of the L452R mutation to the increased binding affinity of these variants to ACE2.
Result: Of note, these two variants have in common the presence of the E484K/Q mutation, with Kappa presenting in addition the L452R substitution.
Result: Our data also support that the RBDs of the Epsilon and Delta variants, which contain the L452R substitution, augment infectivity largely as a result of their improved affinity to the host receptor.
Evaluation of a Rapid and Accessible Reverse Transcription-Quantitative PCR Approach for SARS-CoV-2 Variant of Concern Identification.
PMID: 35465708
2022
Journal of clinical microbiology
Abstract: We designed and analytically validated a two-reaction multiplex reverse transcription-quantitative PCR (RT-qPCR) assay targeting spike protein mutations L452R, E484K, and N501Y in reaction 1 and del69-70, K417N, and T478K in reaction 2.
RBD-mRNA vaccine induces broadly neutralizing antibodies against Omicron and multiple other variants and protects mice from SARS-CoV-2 challenge.
Abstract: The RBD-mRNA-induced antibodies exerted moderate neutralization against authentic B.1.617.2 and B.1.1.529 variants, and pseudotyped B.1.351 and P.1 lineage variants containing K417N/T, E484K, and N501Y mutations, the B.1.617.2 lineage variant harboring L452R, T478K, and P681R mutations, and the B.1.1.529 lineage variant containing 38 mutations in the S protein.
Abstract: The vaccine induced durable antibodies that potently neutralized prototypic strain and B.1.1.7 lineage variant pseudoviruses containing N501Y or D614G mutations alone or in combination with a N439K mutation (B.1.258 lineage)
Delta variant (B.1.617.2) of SARS-CoV-2: Mutations, impact, challenges and possible solutions.
PMID: 35507895
2022
Human vaccines & immunotherapeutics
Abstract: The enhanced transmissibility of Delta variant has been associated with critical mutations such as D614G, L452R, P681R, and T478K in the S-protein.
SARS-CoV-2 spike E156G/Delta157-158 mutations contribute to increased infectivity and immune escape.
Introduction: Indeed, recent reports demonstrated diminished sensitivity of spike PVs bearing L452R and E484Q to BNT162b2 mRNA vaccine-elicited antibodies but a lack of synergy between these two mutations in conferring the resistance.
Introduction: The spike protein from B.1.617 lineage harboring L452R and E484Q mutations was reported to have contributed to the pathogenicity.
Method: All other plasmids expressing spike protein mutants such as pcDNA 3.1 bs(-) T19R, pcDNA 3.1 bs(-) T95I, pcDNA 3.1 bs(-) E156G/Delta157-158, pcDNA 3.1 bs(-) L452R, pcDNA 3.1 bs(-) E484Q, p
Vaccine-Induced Antibody Responses against SARS-CoV-2 Variants-Of-Concern Six Months after the BNT162b2 COVID-19 mRNA Vaccination.
Result: including N501Y in both Alpha and Beta, E484K in Eta and Beta, K417N in Beta, and L452R and T478K only in Delta.
Discussion: Amino acid changes in spike proteins of variants contribute to immune evasion, and it has been suggested that N501Y is associated with increased infectivity, whereas L452R, T478K, and E484K with K417N reduce the interaction of neutralizing antibodies with RBD.
Expansion of L452R-Positive SARS-CoV-2 Omicron Variant, Northern Lombardy, Italy.
Result: 6A), whereas lower density was noticed for the mutations L452R, Discussion: Herein, we studied three critical RBD mutants L452R, E484Q and L452R-E484Q by implementing the all-atom MD simulations to examine the spike glycoprotein molecular alterations associated with RBD mutations.
Discussion: To summarize, the study provided a comprehensive view of destabilizing mechanisms on L452R, E484Q and L452R-E484Q of RBD associated with SARS-CoV-2 spike glycoprotein.
SARS_CoV_2 mutation literature information.
PMID: 
2022
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