Introduction: According to the United States (US) Center for Disease Control (CDC), signature Spike mutations in the aggregated Delta and Delta Plus variant include T19R, (V70F*), T95I, G142D, E156-, F157-, R158G, (A222V*), (W258L*), (K417N*), L452R
Figure: Prevalence of five key mutations (T95I, G142D, R158G, L452R, T478K, and K417N) at different time points in Delta variant (n = 600) sequences and Delta Plus variant (n = 200) sequences.
Introduction: Also, Kappa variant has four S mutations of interest, L452R, E484Q, D614G, and P681R.
Introduction: Delta variant shows four key mutations in sequence encoding S protein: L452R, T478K, D614G, P681R.
Introduction: The L452R mutation increases protein stability, viral infectivity, and potentially promotes viral replication.
Introduction: The L452R mutation is within the S RBD, and thus may be relevant to transmissibility or immune escape.
Real-time reverse transcription-polymerase chain reaction assay panel for the detection of severe acute respiratory syndrome coronavirus 2 and its variants.
Discussion: In addition, there are some other significant mutations in SARS-CoV-2 variants, such as D614G, L452R, and E484Q, which can also be considered for specific detection with rRT-PCR assay; relevant research in our laboratory is in progress.
The Emergence and Spread of Novel SARS-CoV-2 Variants.
Result: L452R, located in RBM, may increase infectivity by enhancing the binding of S protein to ACE2 receptor and evading neutralizing antibodies and has evolved independently in multiple lineages.
Result: The mutations of S protein include S13I, W152C, and L452R.
Table: L452R
Emergence and expansion of SARS-CoV-2 B.1.526 after identification in New York.
Introduction: Phylogenetic examination showed that the B.1.526 lineage comprises two closely related sub-lineages harbouring either E484K (B.1.526-E484K; defined as Pangolin lineage B.1.526) or S477N (B.1.526-S477N; Pangolin lineage B.1.526.2), and the additional sub-lineage B.1.526.1, harbouring the
Figure: Phylogenetic tree based on whole-genome alignment of genomes sequenced from our hospital centre with at least one mutation of interest or concern (E484K, N501Y, S477N, or L452R) and unique spike protein mutation constellations (n = 64).
Figure: The B.1.526-L452R sub-lineage (green) emerged in parallel.
Epitope diversity of SARS-CoV-2 hyperimmune intravenous human immunoglobulins and neutralization of variants of concern.
Method: Antibody preparations were evaluated by SARS-CoV-2 pseudovirus neutralization assay (PsVNA) using WA-1 strain, UK variant (B.1.1.7 with spike mutations: H69-V70del, Y144del, N501Y, A570D, D614G, P681H, T716I, S982A, and D1118H), SA variant (B.1.351 strain with spike mutations L18F, D80A, D215G, L242-244del, R246I, K417N, E484K, N501Y, D614G, and
Single-Amplicon Multiplex Real-Time Reverse Transcription-PCR with Tiled Probes To Detect SARS-CoV-2 spike Mutations Associated with Variants of Concern.
PMID: 34432488
2021
Journal of clinical microbiology
Abstract: Subsequently, a fourth probe was designed to detect L452R.
Introduction: These lineages, many of which share common mutations in the spike protein (e.g., N501Y, E484K and L452R), have been declared variants of concern (VOC) by public health authorities (https://www.cdc.gov/coronavirus/2019-ncov/variants/variant-info.html).
Discussion: In California, use of a targeted SNP assay allowed for real-time surveillance of the emergence of variants harboring the L452R mutation.
Discussion: The simple design of the SNP assay provides consistent amplification of the target region, limits the potential for amplicon dropout from mutations in the primer sequences, and facilitates the addition of new probes to detect emerging mutations identified among SARS-CoV-2 variants
ACE2-targeting monoclonal antibody as potent and broad-spectrum coronavirus blocker.
PMID: 34433803
2021
Signal transduction and targeted therapy
Community-level SARS-CoV-2 sequence diversity revealed by wastewater sampling.
PMID: 34438144
2021
The Science of the total environment
Table: L452R
Molecular Dynamics Simulation Study of the Interaction between Human Angiotensin Converting Enzyme 2 and Spike Protein Receptor Binding Domain of the SARS-CoV-2 B.1.617 Variant.
Conclusion: The L452R mutation enhances the electrostatics of the binding surface and aids electrostatic attraction between hACE2 and the S protein.
Result: A change from a hydrophobic leucine on the protein surface to arginine (L452R) also increases its interactions with water molecules that could further stabilize the protein.
Result: Besides these interactions, residues of single mutant L452R, Tyr489 and Gly496 of S protein, interacted with Gln24 and Lys353 of hACE2, respectively (Figure 4A).
Result: However, as expected, this salt bridge was observed in the L452R single mutant complex (Figure 4A).
Result: In support of our results, Cherian and colleagues reported that the L452R mutation, and