Introduction: However, there have been several mutations reported in SARS-CoV-2 RBD, such as N501Y, L452R, S477N, E484K, A502S, N439K, S494P, T478K, K417N, and K417T.
Antibody-Mediated Neutralization of Authentic SARS-CoV-2 B.1.617 Variants Harboring L452R and T478K/E484Q.
Abstract: Both B.1.617 variants Kappa (+E484Q) and Delta (+
Conclusion: SARS-CoV-2 Kappa variant harboring E484Q mediate resistance to casirivimab while the substitution T478K present in Delta results in limited neutralization by imdevimab.
Introduction: In Delta, in close proximity to E484, a threonine is replaced by a positively charged lysine leading to T478K.
Introduction: Little is known so far about the clinical relevance of the newly emerging T478K substitution.
Introduction: Whether T478K or E484Q, respectively, contribute to immune evasion similar to the E484K mutation is of great therapeutic importance as well as for evaluating the efficacy of currently approved vaccines.
Clinical Characterization and Genomic Analysis of Samples from COVID-19 Breakthrough Infections during the Second Wave among the Various States of India.
Result: Common in B.1.617.2 lineage: ORF1ab P4715L; spikeT19R, L452R, T478K, D614G, and P681R; ORF3a S26L; M I82T; ORF7a V82A and T120I; and N D63G, R203M, and D377Y.
A rapid screening assay for L452R and T478K spike mutations in SARS-CoV-2 Delta variant using high-resolution melting analysis.
PMID: 34602531
2021
The Journal of toxicological sciences
Abstract: In addition, HRM analysis distinguished the T478K mutant from the wild-type T478.
Abstract: In this assay, we determined L452R and T478K, among which T478K is an identifier of the Delta variant since L452R is seen in other strains (Kappa and Epsilon variants).
Abstract: Seven clinical samples containing the Delta variant were successfully identified as L452R/T478K mutants.
Evaluation of the clinical and analytical performance of the Seegene allplex SARS-CoV-2 variants I assay for the detection of variants of concern (VOC) and variants of interests (VOI).
Figure: (a) Binding responses of anti-SARS-CoV-2 S protein mAbs, S1D2-hIgG1, STI-1499-LALA and 1741-LALA to the S1 fragment of the S protein from SARS-CoV-2 variants, including 2019-nCoV, B.1.1.7 (HV69-70 deletion, Y144 deletion, N501Y, A570D, D614G, P681H)-, B.1.351 (K417N, E484K, N501Y, D614G)-, and B.1.617.2 (T19R, G142D, E156G, 157-158 deletion, L452R, T478K, D614G, P681R)- lineage.
SARS-CoV-2 Virus-Host Interaction: Currently Available Structures and Implications of Variant Emergence on Infectivity and Immune Response.
PMID: 34639178
2021
International journal of molecular sciences
Discussion: Regarding infectivity, this strain possesses mutation D614G and one mutation in the RBD, T478K.
Structure-Function Analysis of Resistance to Bamlanivimab by SARS-CoV-2 Variants Kappa, Delta, and Lambda.
PMID: 34648284
2021
Journal of chemical information and modeling
Abstract: The newly emerging Kappa, Delta, and Lambda SARS-CoV-2 variants are worrisome, characterized with the double mutations E484Q/L452R, T478K/L452R, and F490S/L452Q, respectively, in their receptor binding domains (RBDs) of the spike proteins.
Result: Compared with the free energy change for the T478K mutation in the free state (i.e., the RBD alone), in the bound state (i.e., the complex of RBD and LY-CoV555), the free energy change for the same mutation is larger only by 0.70 kcal/mol, which suggests that the T478K mutation mo
Spike protein evolution in the SARS-CoV-2 Delta variant of concern: a case series from Northern Lombardy.
Introduction: The Delta VOC, identified in October 2020 in India, consists of 41 different sublineages sharing additional T19R, del157/158, T478K, and D950N in Spike protein and I82T in M protein compared to B.1.
Bioinformatics analysis of the differences in the binding profile of the wild-type and mutants of the SARS-CoV-2 spike protein variants with the ACE2 receptor.
PMID: 34655895
2021
Computers in biology and medicine
Introduction: A detailed, systematic, and comprehensive investigation is essential to determine how the N439K, S477 N, and T478K substitutions affect the binding of the spike protein with the ACE2 receptor and initiate structural and functional changes.
Introduction: In the present study, we used different theoretical and computational methods such as protein-protein docking, molecular dynamics simulations, and binding free energy calculations to investigate the structural changes that (1) alter the binding between RDB and ACE2 receptor as a result of N439K, S477 N, and T478K mutations, and (2) increase the infectivity rates.
SARS_CoV_2 mutation literature information.
PMID: 
2021
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