Introduction: 1d, the L452R and P681R mutations were highly conserved in the B.1.617 lineage and, notably, the P681R mutation (16,650 out of 16,759 sequences, 99.3%) was the most representative mutation in this lineage.
Method: However, the S protein of this viral sequence (GISAID ID: EPI_ISL_2220643) possesses neither L452R nor P681R mutations, both of which are features of the B.1.617 lineage.
Highly sensitive and specific detection of the SARS-CoV-2 Delta variant by double-mismatch allele-specific real time reverse transcription PCR.
Abstract: The technique exploits allele-specific primers, targeting two spike gene mu
Introduction: In contrast, the double-mismatch allele-specific real time RT-PCR (DMAS-RT-PCR) method that we describe here does not exhibit such non-specificity because it targets two separate Delta spike gene mutations, L452R and T478K, within the same amplicon.
Method: Some of these individual mutations are shared by other variants but we noted that the combination of spike mutations L452R and T478K (nucleotide positions T22917G and C22995A, respectively) within the receptor binding domain can effectively differentiate Delta from other variants.
Surveillance of SARS-CoV-2 variants of concern by identification of single nucleotide polymorphisms in the spike protein by a multiplex real-time PCR.
PMID: 34822912
2022
Journal of virological methods
Abstract: RESULTS: Of the 664/934 that were subjected to the multiplex qRT-PCR, 638 (96.1
Result: 638 (96.1 %) samples showed amplification for the genes targeting L452R and K417 and therefore, were considered to be the delta variant.
Result: We also tested 20 samples that were assigned the delta lineage by sequencing and the only genes targeting L452R was amplified.
Discussion: However, in situations where there is a dominant variant with L452R or N501Y, confirmed by whole genomic sequencing, this would be an easy to use, low-cost assay to rapidly identify the prevalence of VOCs such as delta.
Discussion: However, the SNPs resulting in L452R and K417 mutations is not unique to delta alone and is detected in several variants of interest such as Kappa (B.1.617.1), Epsilon (B.1.427/9) and C.36.
Reduced sensitivity of the SARS-CoV-2 Lambda variant to monoclonal antibodies and neutralizing antibodies induced by infection and vaccination.
Introduction: The L452R mutation found in the Delta, Kappa, and Epsilon variants has been reported to enhance viral infectivity and fusogenicity while promoting viral replication.
Discussion: In addition, our previous studies revealed that escape of the L452R and E484 K mutants from mAbs frequently occurred in conjunction.
Discussion: Our previous study found that the L452R and F490L mutations can cause escape from mAb X593, consistent with the results of the L452Q and F490S mutations in the present study.
Discussion: Our previous study showed that both F490 and L452 are located at the binding site of mAb 9G11 to the RBD, and experimentally verified that F490L
In vitro data suggest that Indian delta variant B.1.617 of SARS-CoV-2 escapes neutralization by both receptor affinity and immune evasion.
Result: Anti-RBD IgG ELISA shows that antibodies induced by infection with wild-type Wuhan SARS-CoV-2 fail to recognize the RBD mutants L452R/E484Q (variant B.1.617) and E484K (variants P.1 and B.1.351), while recognition of RBDN440K is unaltered.
Result: Binding kinetics of RBD mutants to ACE2 show increased affinity due L452R/E484Q and E484K mutations.
Result: In contrast to direct binding of immune sera to RBD, inhibition of the RBD-ACE2 interaction was more severely affected and reduced for all mutations, most notably E484K<
A comprehensive overview of identified mutations in SARS CoV-2 spike glycoprotein among Iranian patients.
Introduction: While most of alterations in the receptor binding domain (RBD) reduce infectivity, A475V, L452R, V483A, and F490L variants induce resistance to some neutralizing antibodies.
Table: L452R
Discussion: L452R, T478K, N501Y and S477N have been the most frequently detected mutations in RDB.
Emergence of a novel SARS-CoV-2 Pango lineage B.1.1.526 in West Bengal, India.
PMID: 34896696
2022
Journal of infection and public health
Introduction: Along with the clade specific mutations, these variants have their own sets of characteristics mutations including several mutations in the S glycoprotein like Delta69-70, Delta144-145, N501Y, A570D, P681H, T716I, S982A, D1118H in the Alpha variant; D80A, D215G, Delta241-243, K417N, E484K, N501Y, A701V in the Beta variant; L18F, T20N, P26S, D138Y, R190S,
Longitudinal analysis of SARS-CoV-2 spike and RNA-dependent RNA polymerase protein sequences reveals the emergence and geographic distribution of diverse mutations.
PMID: 34801754
2022
Infection, genetics and evolution
Result: 5D) share the same set of mutations on the spike protein (S13I,
Figure: L18F, E484K, N501Y, D614G, H655Y, and V1176F are associated with the Gamma variant of concern, and S13I, W152C, L452R are associated with the Epsilon variant of concern.
Figure: The substitution L452R is observed in the Epsilon variant of concern.
Figure: The substitutions L452R and S13I appeared separately before the emergence of the variant, while W152C did not.
Efficacy of mRNA, adenoviral vector, and perfusion protein COVID-19 vaccines.
Introduction: Consequently, ten mutations in the spike protein of B.1.617.2 strain, including T19R, (G142D*), 156/157del, R158G, L452R, T478K, D614G, P681R, and D950N were identified.
Table: L452R
E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.
PMID: 34915409
2022
International immunopharmacology
In
Introduction: N439K, L452R, and Y453F showed an increase in ACE2 receptor binding ability.
Introduction: Currently, there are four variants of concerns: Alpha variant (B.1.1.7; RBD mutations: N501Y, A570D), Beta (B.1.351; RBD mutations: K417N, E484K, and N501Y), Gamma (P.1, B.1.1.28.1; RBD mutations: K417N/T, E484K, and N501Y) and Delta (B.1.617.2; RBD mutations: L452R, T478K).
SARS_CoV_2 mutation literature information.
PMID: 
2022
Nature
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