SARS_CoV_2 mutation literature information.


  The Delta Variant Mutations in the Receptor Binding Domain of SARS-CoV-2 Show Enhanced Electrostatic Interactions with the ACE2.
 PMID: 34901826       2021       Medicine in drug discovery
Abstract: Recently, a new strain is reported in India that includes a mutation (T478K, and L452R) in the RBD, that is possibly increasing the infection rate.
Introduction: Besides, L452R mutation recently reported to enhance the viral replication by increasing the S protein stability and viral infectivity and viral fusogenicity.
Introduction: In contrary to T478K, the L452R variant is shown to enhance the total binding energy between RBD and ACE2 to be about 2.63 kcal/mol more negative than its value in WT protein.


  Development of an efficient Sanger sequencing-based assay for detecting SARS-CoV-2 spike mutations.
 PMID: 34905589       2021       PloS one
Abstract: Here, we developed five SARS-CoV-2 spike gene primer pairs (5-SSG primer assay; 69S, 144S, 417S, 484S, and 570S) and verified their ability to detect nine key spike mutations (DeltaH69/V70, T95I, G142D, DeltaY144, K417T/N, L452R, E484K/Q, N501Y, and H655Y) using a Sanger sequencing-based assay.


  Loss of Neutralizing Antibody Response to mRNA Vaccination against SARS-CoV-2 Variants: Differing Kinetics and Strong Boosting by Breakthrough Infection.
 PMID: 34909777       2021       bioRxiv
Introduction: Finally, Delta (B.1.617.2) is responsible for the most recent wave of the COVID-19 pandemic and is characterized by new NTD alterations, together with key RBD mutations (L452R and T478K).


  Hotspot Mutations in SARS-CoV-2.
 PMID: 34912372       2021       Frontiers in genetics
Abstract: In addition to this, SSIPe is used to report the binding affinity between the receptor-binding domain of Spike protein and human ACE2 protein by considering L452R, T478K, E484Q, and N501Y hotspot mutations in that region.
Conclusion: Finally, SSIPe is used to report the binding affinity between the RBD of Spike protein and human ACE2 protein by considering L452R,
Introduction: On the other hand, the variant B.1.617.2 was first identified in India with L452R, T478K, D614G, and P681R mutations in Spike glycoprotein.


  Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding.
 PMID: 34914928       2021       Cell reports
Discussion: Although there are many factors governing viral evolution, these results suggest that the independent evolution of L452R-bearing spikes and N501Y-, K417N/T-, and E484K-bearing spikes may be explained by a lack of synergistic increase in ACE2 binding upon combination of these mutations.
Discussion: Although these mutational combinations enable enhanced ACE2 binding compared with wild-type spikes, the increase in ACE2 binding affinity conferred by the L452R mutation in isolation was not preserved.
Discussion: As L452 is distal to the ACE2-RBD interface, it has been previously suggested that the L452R mutation may increa


  Glycan Masking of Epitopes in the NTD and RBD of the Spike Protein Elicits Broadly Neutralizing Antibodies Against SARS-CoV-2 Variants.
 PMID: 34925381       2021       Frontiers in immunology
Introduction: The Delta (B.1.617.2) variant encodes an S protein with ten mutations (T19R, G142D, del 156, del 157, R158G, L452R, T478K, D614G, P681R, and D950N), two of which are in the RBD (L452R and T478K).
Introduction: The immunity-evading mutations in the Beta (B1.351) variant include E484K in the RBD of the S protein, while those in the Delta (B.167.2) variant include L19R, del 157, del 158, L452R


  The Development of SARS-CoV-2 Variants: The Gene Makes the Disease.
 PMID: 34940505       2021       Journal of developmental biology
Introduction: L452R, defined as an escape mutation, has been shown to promote a much higher viral replication in non-human cell cultures, which would correspond with the better fitness of the Delta variant observed in populations.
Introduction: It is characterized by the L452R mutation, which was expected to give an advantage when spreading over other variants, being more contagious than earlier forms.
Introduction: The ancestral lineage B.1.617 is not a variant but a cluster of sequences within clade G that share the common signature mutations: G142D, L452R, E484Q, D614G, and P681R.


  Insights into the Binding of Receptor-Binding Domain (RBD) of SARS-CoV-2 Wild Type and B.1.620 Variant with hACE2 Using Molecular Docking and Simulation Approaches.
 PMID: 34943225       2021       Biology
Introduction: In contrast, the delta+ variant acquired an additional mutation, the K417N mutation, alongside the L452R and T478K mutations.
Introduction: The Kappa (kappa) variant, also known as B.1.617.1, first identified in India, and designated as a VOI, owns a single mutation, that is, L452R, which was suspected to be associated with reduced antibody neutralization by disrupting the respective conformational epitopes.
Introduction: To date, many variants have been reported, among which the VOC Delta (delta)+ (AY.1 or lineage B.1.617.2.1), which evolved from Delta, demonstrated a different mutational landscape by acquiring L452R and T478K mutations in the RBD.


  Computational Saturation Mutagenesis of SARS-CoV-1 Spike Glycoprotein: Stability, Binding Affinity, and Comparison With SARS-CoV-2.
 PMID: 34957216       2021       Frontiers in molecular biosciences
Result: Recent SARS-CoV-2 variant L452R ( G = -0.395 kcal/mol; G = 0.021 kcal/mol) corresponds to SARS-CoV-1 K439R ( G = 0.247 kcal/mol; G = 0.41 kcal/mol).
Result: The change in residue from Lysine in SARS-CoV-1 S protein to Leucine in SARS-CoV-2 S protein may be responsible for the increase in binding affinity caused by L452R.


  SARS-CoV-2 Delta Variant Displays Moderate Resistance to Neutralizing Antibodies and Spike Protein Properties of Higher Soluble ACE2 Sensitivity, Enhanced Cleavage and Fusogenic Activity.
 PMID: 34960755       2021       Viruses
Result: A further reduction in neutralization titers was seen against pseudoviruses bearing both L452R and T478 substitutions in RBD displayed (GMT 192) compared to WT(D614G) (GMT 392).
Result: A prior study showed that convalescent sera and vaccine-elicited antibody neutralization titers against pseudoviruses bearing spikes containing L452R-E484Q-P681R substitutions displayed 2-5-fold reduction, compared to the neutralization titers against WT(D614G) pseudoviruses.
Result: Again, pseudoviruses K417N, L452R, T478K, L452Q + F490S



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