Introduction: The B.1.429 variant, a lineage recently emerged in California, United States, contains 4 missense mutations in spike including a single L452R RBD mutation.
Result: RBD L452R mutation from B.1.429 variant leads to a slightly increased neutralization resistance of these RmAbs.
2020 SARS-CoV-2 diversification in the United States: Establishing a pre-vaccination baseline.
Introduction: Mutations defining the B.1.427/429 VOC (SS13I;W152C;L452R) which originated in the U.S., were only detected in a very small fraction of sequences in Dec 2020, possibily due to the lag between sample collection and sequence deposition and/or shallow Phase 3 sampling.
An ACE2 Triple Decoy that neutralizes SARS-CoV-2 shows enhanced affinity for virus variants.
Abstract: The ACE2 Triple Decoy maintains high affinity for mutated S RBD, displays enhanced affinity for S RBD N501Y or L452R, and has the highest affinity for S RBD with both E484K and N501Y mutations, making it a viable therapeutic option for the prevention or treatment of SARS-CoV-2 infection with a high likelihood of efficacy against variants.
Introduction: This ACE2 Triple Decoy not only maintained affinity for variant S RBD, it showed an increased affinity for S&nb
Rational optimization of a human neutralizing antibody of SARS-CoV-2.
PMID: 34147856
2021
Computers in biology and medicine
Result: The results indicate the binding affinity of WT P2B-2F6 remains almost unchanged with most single spike protein mutants except for E484K and L452R.
Table: L452R
Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.
Result: A second group of RBD variants, L452R (15%), G446V (10%), and N440Y (5%) disrupted fewer NAb interactions, while all NAbs bound efficiently (>50%, relative to WT reference) to RBD variants T345I, A475V, and Y505W.
Result: Additional conserved RBD contacts within the C2 NAb epitope suggests RBD variants G446V, L452R, and S494P can also impact C2 interactions.
Result: Based on the in silico NAb epitope analysis, nine RBD variants that localize to the C1 ( PMID: 34159336
2021
bioRxiv
Abstract: Structural modeling supported potential functional impact of the D1118H and L452R mutations.
Result: The L452R mutation is situated in the RBD; homology modelling of the RBD-ACE2 complex shows that while R452 does not directly contact ACE2, the guanidinium side chain of R452 is surface-exposed and thus could potentially impact nAb binding.
Result: The L452R mutation was recently shown to reduce binding affinity to some RBD-targeting monoclonal antibodies, as well as to reduce susceptibility to nAbs.
Result: The VRV-haplotype S13I-W152C-L452R (ICR-3) appeared in Fall 2020 and is rapidly becoming dominant in state
Preliminary Structural Data Revealed That the SARS-CoV-2 B.1.617 Variant's RBD Binds to ACE2 Receptor Stronger Than the Wild Type to Enhance the Infectivity.
Abstract: In this study, we used structural and biomolecular simulation techniques to explore the impact of specific mutations (L452R<
Result: The RBD-specific mutations (L452R-E484 K) reported in India requires careful examination in the search for new therapeutic alternatives.
Result: This study was conducted to explore the binding differences of the spike RBD of the wild and B.1.617 variant (L452R-E484Q) with the host ACE2 by using combined structural modelling and biophysical approaches.
Result: We concluded that L452R-E484Q mutations and other factors such as genetic variability in the other proteins might help the virus enforce infection and its severity.
SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity.
Introduction: Furthermore, we artificially generated SARS-CoV-2 harboring these point mutations by reverse genetics and show that the L452R mutant enhances viral replication capacity.
Introduction: More intriguingly, the L452R and Y453F mutants enhance binding affinity for ACE2, and experiments using pseudoviruses show that the L452R substitution increases viral infectivity.
Introduction: We demonstrate that at least two naturally occurring substitutions in the receptor-binding motif (RBM; residues 438-506) of the SARS-CoV-2 S protein, L452R and Y453F, which were identified in the two major variants, B.1.427/429 (L452R) and B1.1.298 (Y453F), can be resistant to cellular
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Introduction: In January 2021, the emergence of a novel variant in California carrying an L452R mutation in the RBD was reported.
Introduction: In addition, the combination of L452R and E484Q was not shown to have an additive effect; rather, the loss of sensitivity was similar to that observed with each mutation individually.
Introduction: It is characterized by spike mutations T19R, G142D, Delta157-158, L452R, T478K, D614G, P681R, and D950N (Figure 3).
Introduction: The impact on the immune escape capacity of three sublineages of B.1.617 is expected, owi
Anti-SARS-CoV-2 Vaccines and Monoclonal Antibodies Facing Viral Variants.
Introduction: However, the presence of L452R could be involved in the decrease in antibody activity, and the E484Q could affect vaccine efficiency.
Introduction: It carries mutations in NSPs and on some ORF proteins, in addition to two key mutations on RBD: L452R common to the CAL.20C variant and E484Q close to the E484K observed in some VOCs.
Introduction: It derives from the B line (B.1.429 and B.1.427) and carries three mutations on the Spike: S13I, W152C, and, most notably, L452R, located in the RBD and potentially involved in mAbs neutralization escape (Table 1).
SARS_CoV_2 mutation literature information.
PMID: 
2021
Emerging microbes & infections
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