literature

SARS_CoV_2 mutation literature information.

Role of the Microbiome in the Pathogenesis of COVID-19.

PMID: 35433495 2022 Frontiers in cellular and infection microbiology

Table: L452R

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.

PMID: 35401825 2022 Theranostics

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

Unique peptide signatures of SARS-ComicronV-2 virus against human proteome reveal variants' immune escape and infectiveness.

PMID: 35399374 2022 Heliyon

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.

Immune evasion and chronological decrease in titer of neutralizing antibody against SARS-CoV-2 and its variants of concerns in COVID-19 patients.

PMID: 35398519 2022 Clinical immunology (Orlando, Fla.)

Introduction: This lineage has three main subtypes: B.1.617.1 (Kappa variant) and B.1.617.3, characterized by L452R and E484Q mutation in RBD, and B.1.617.2 (Delta variant), characterized by L452R and T478K in RBD.

Emergence and phenotypic characterization of the global SARS-CoV-2 C.1.2 lineage.

PMID: 35396511 2022 Nature communications

Method: The SARS-CoV-2 Wuhan-1 spike, cloned into pCDNA3.1, was mutated using the QuikChange Lightning Site-Directed Mutagenesis kit (Agilent Technologies) and NEBuilder HiFi DNA Assembly Master Mix (NEB) to include D614G (wild-type) or lineage defining mutations for Beta (L18F, D80A, D215G, 241-243del, K417N, E484K, N501Y, D614G and A701V), Delta (T19R, 156-157del, R158G, L452R, T478K, D614G, P681R and D950N

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,

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

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.

High-resolution melting analysis after nested PCR for the detection of SARS-CoV-2 spike protein G339D and D796Y variations.

PMID: 35349821 2022 Biochemical and biophysical research communications

7Figure: (B) Normalized HRM curves of amplicons from the second amplification by nested PCR with the primer pair ""Second L452R fo

8Discussion: Therefore, a pair of ""Second L452R forward"" and ""Second L452R reverse"" primers was not suitable to detect mutations in RBD nt 22852-22956."

8Discussion: We employed the same primer pair (""Second L452R forward"" and ""Second L452R reverse"" in Supplementary Table 1) as reported by Aoki et al."

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