Abstract: Extensive analysis has indicated that the critical P681R mutation produces new C/H-CrUPs around the R685 cleavage site, while the L452R mutation causes loss of antigenicity of the NF9 peptide and strong(er) binding of the virus to its ACE2 receptor protein.
Result: Interestingly, related studies have shown that the L452R mutation (and subsequently the new created C/H-CrUPs herein characterized) increases the infectiveness of SARS-CoV-2, by strengthening the electrostatic interactions of this region on Spike protein with the ACE2 virus receptor.
Result: Mutation analysis indicated that in the NF9 peptide the mutation L452R is carried by the variants Alpha, Delta, Lamda and Kappa, while the mutation L452Q appears in the variant Lambda.
Result: The mutation
Comparative genomics, evolutionary epidemiology, and RBD-hACE2 receptor binding pattern in B.1.1.7 (Alpha) and B.1.617.2 (Delta) related to their pandemic response in UK and India.
PMID: 35427787
2022
Infection, genetics and evolution
Abstract: First, we served comparative genomics, such as genome sequence submission patterns, mutational landscapes, and structural landscapes of significant mutations (N501Y, D614G, L452R, E484Q, and P681R).
Abstract: The structural pattern was analyzed in the N501Y, D614G L452R, E484Q, and P681R mutations.
Introduction: L452R is related to a reduction in therapeutic antibodies and is ass
Introduction: Among these three mutations, L452R and E484Q are located in the RBD region.
Expansion of L452R-Positive SARS-CoV-2 Omicron Variant, Northern Lombardy, Italy.
Abstract: Many laboratories are using previously developed L452R-specific PCRs to discriminate Omicron from Delta mutations, but these tests may be unreliable.
Abstract: We report 25 cases of infection with SARS-CoV-2 Omicron variant containing spike protein L452R mutation in northern Lombardy, Italy.
Differences in Transmission between SARS-CoV-2 Alpha (B.1.1.7) and Delta (B.1.617.2) Variants.
Abstract: In index cases, Spike gene target failure (TaqPath) was used as a proxy of Alpha variant and the L452R mutation (TaqMan) for Delta variant.
Method: The detection of the L452R mutation by TaqMan assay was used as a proxy measure of the Delta variant.
Increased Secondary Attack Rate among Unvaccinated Household Contacts of Coronavirus Disease 2019 Patients with Delta Variant in Japan.
PMID: 35409572
2022
International journal of environmental research and public health
Abstract: We studied household contacts of index cases of COVID-19 infected with Delta (L452R mutation), Alpha (N501Y mutation), and wild strain from December 2020 through November 2021 in Itako, Japan.
Method: Among unvaccinated COVID-19 contacts, we defined contact of the index case with the L452R variant among the patients or their contacts as contacts of the Delta variant.
Method: Contact with the Alpha strain was defined as contact of the index patient with positive results for N501Y mutation until 20 June 2021 or negative results for
Discussion: Last, the Delta and Alpha variants were mainly confirmed by the L452R and N501Y mutations, respectively.
Cocktail of REGN Antibodies Binds More Strongly to SARS-CoV-2 Than Its Components, but the Omicron Variant Reduces Its Neutralizing Ability.
PMID: 35403431
2022
The journal of physical chemistry. B
Result: This is because the L452R and T478K mutations do not significantly contribute to the REGN10933-RBD stability, as their total interaction energy varies from -0.5 and -3.4 kcal/mol (WT) to 0.4 and -3.5 kcal/mol (Delta) (Table 4).
Inhibitor screening using microarray identifies the high capacity of neutralizing antibodies to Spike variants in SARS-CoV-2 infection and vaccination.
Result: An additional five mutations had <= 2-fold increased binding to human ACE2 (Figure 2C-D): L452R (in B.1.427/429 and B.1.617), Y453F (in B.1.1.298), E484Q (in B.1.617.1 and B.1.617.3) and N501Y (in B.1.1.529, B.1.1.7, B.1.351 and P.1).
Result: The most prevalent D614G mutation and some mutations of interest (i.e., N501Y, L452R, K417N, N439K, S477N, S494P) were among the variants printed.
Discussion: The S variants tested here contain mutations that were selected from the COVID-19 virus mutation tracker database and
Insights from computational analysis: how does the SARS-CoV-2 Delta (B.1.617.2) variant hijack ACE2 more effectively?
PMID: 35364605
2022
Physical chemistry chemical physics
Abstract: The results showed that the existence of L452R and T478K mutations can trigger the effective hijacking of ACE2 by the Delta variant through the following three ways: (i) these two mutations can significantly enhance the electrostatic energy of the system by the introduction of two positively charged amino acids (Arg and Lys), thereby increasing the binding affinity of RBD and ACE2, (ii) the Loops 1, 3, and 4 in the receptor-binding motif (RBM) of RBD form a tighter conformation under the dominance of the T478K mutation, allowing ACE2 to be captured more effectively than the wild-type system, and (iii) these conformational changes lead to a more stable hydrogen bond in the Delta variant, which further ensures the stability of the binding.
Impact of B.1.617 and RBD SARS-CoV-2 variants on vaccine efficacy: An in-silico approach.
PMID: 35370005
2022
Indian journal of medical microbiology
Introduction: Two mutations in the RBD (L452R, E484Q), the area important for viral entry, are present in this variation.
Result: We found that seven mutant variants (F486L, Q493N, B.1.617 (L452R & E484Q), R408I, L455Y, K417G and E484K) have structural changes in RBD region (S3).
Table: L452R
SARS-CoV-2 BA.1 variant is neutralized by vaccine booster-elicited serum, but evades most convalescent serum and therapeutic antibodies.
PMID: 35380448
2022
Science translational medicine
Result: We compared the neutralization titers of these serum samples against pseudoviruses bearing spike proteins from the following variants: D614G, Omicron (A67V, del69-70, T95I, del142-144, Y145D, del211, L212I, ins214EPE, G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R,
SARS_CoV_2 mutation literature information.
PMID: 
2022
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