3Introduction: L452R is also the main mutation in the ""Epsilon variant"" B.1.429 and is related to an increase in the viral load and an approximately 20% increase in transmissibility."
Introduction: Compared with the D614G mutation alone, the ability of a pseudovirus carrying the L452R mutation to infect 293T cells increases by 6.7-22.5 times and the ability to infect HAO-ACE2 cells increases by 5.8-14.7 times.
Introduction: Several independent lineages carrying L452R have been reported in the global GISAID database, suggesting that the L452R mutation alone is of significant adaptive value to SARS-CoV-2.
Introduction: The Delta variant contains L452R, T478K, D614G, and PMID: 34499599
2021
Emerging infectious diseases
Introduction: This variant of concern (VOC) was renamed Delta by the World Health Organization and consists to date of 5 different sublineages (B.1.617.2, AY.1, AY.2, AY.3, and AY.3.1, according to PANGOLIN phylogeny) that share T478K and L452R as the main mutations of concern (MOCs) within the spike protein.
Possible Link between Higher Transmissibility of Alpha, Kappa and Delta Variants of SARS-CoV-2 and Increased Structural Stability of Its Spike Protein and hACE2 Affinity.
PMID: 34502041
2021
International journal of molecular sciences
Introduction: All these lineages have conserved L452R, D614G and P681R (accessed on 6 June 2021).
Introduction: As in lineage B.1.617, Kappa and B.1.617.3 have same L452R and E484Q mutation in RBD of spike, while Delta has L452R and T478K, we have only considered Kappa and Delta in this study.
Introduction: The Kappa is characterized by E154K, L452R, E484Q, D614G, P681R, Q1071H mutations in the spike protein and Delta by
Dynamics prediction of emerging notable spike protein mutations in SARS-CoV-2 implies a need for updated vaccines.
Abstract: It was found that the mutations, Leu452Arg, Thr478Lys, and Glu484Gln in the spike protein increase the affinity for the hACE2 receptor, which explains the greater infectivity of the SARS-Cov-2 B.1.617 (Indian Variant).
Introduction: In the Delta variant, the mutations found in its RBD are L452R and T478K.
Introduction: In the present study, we have focused on the Delta and Kappa variants and utilized homology modeling (HM) simulations of S protein trimer to assess its dynamic behavior in terms of conformational stability as well as the interaction of isolated viral RBD in complex with human ACE2 to probe the specific interactions emanating from the double mut
Result: First, the 10 most observed or fast-growing RBD mutations are N501Y, L452R, T478K, E484K, K417T, S477N, N439K, K417N, F490S, and S494P, as shown in Table 1.
Result: Four RBD mutations, N501Y, L452R, F490S, and L452Q, appear in both lists and are key mutations in WHO's VOC and VOI lists.
Result: From Figure 2, RBD 2 co-mutation set [L452R, <
Contribution of single mutations to selected SARS-CoV-2 emerging variants spike antigenicity.
Result: Interestingly, the L452R mutant did not have a major impact in ACE2 affinity when tested in the context of recombinant monomeric RBD.
Result: On the other hand, its RBD mutation, L452R, increased ACE2-Fc binding by ~2.7 folds, suggesting its major contribution to the phenotype of this variant.
Result: The RBD mutation L452R also presented a minor ~1.16-fold decrease in recognition by plasma from vaccinated individuals.
Result: While our results identified some key mutations enhancing ACE2 interaction (i.e., N501Y, L452R and mutation/deletion in the NTD), the overall increased ACE2 affinity from any given variant appears to result from more than the sum of the effect of individual muta
Review of the mechanisms of SARS-CoV-2 evolution and transmission.
Introduction: A list of vaccine-escape (vaccine-breakthrough) mutations was tabulated in our early work, including S494P, Q493L, K417N, F490S, F486L, R403K, E484K, L452R, K417T, F490L, E484Q, and A475S.
Introduction: Additionally, although their frequencies are relatively low at present, co-mutation sets [L452R, T478K, E484K, N501Y] and [P384L, K417N,
Rapid Identification of Neutralizing Antibodies against SARS-CoV-2 Variants by mRNA Display.
Abstract: A potent ACE2-blocking nAb was further engineered to sustain binding to S RBD with the E484K and L452R substitutions found in multiple SARS-CoV-2 variants.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Nature
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