Introduction: By analyzing the frequency, binding free energy (BFE) changes, and antibody disruption counts of RBD comutations, we reveal that nine RBD comutation sets, namely [L452R, T478K], [L452Q, F490S], [E484K, N501Y
Method: In our predictions, L452R induces a negative BFE change (-2.39 kcal/mol), and T478K produces a positive BFE change (0.36 kcal/mol).
Method: Recent studies on potency of mAb CT-P59 in vitro and in vivo against Delta variants show that the neutralization of CT-P59 is reduced by L452R (13.22 ng/mL) and is retained against T478K (0.213 ng/mL).
Mass Screening of SARS-CoV-2 Variants using Sanger Sequencing Strategy in Hiroshima, Japan.
Method: 2 literally having K417N, T478K, E484A and N501Y mutation in the Sanger sequences.
Method: If we found the mutation from Guanine (G) to Adenine (A) or Cystine (C)at nt23012, further identification was done as follows: double mutation of T22917G (referred to L452R) and C22995A (referred to T478K) for B.1.617.2 (Delta), T22917G (referred to L452R) and G23012C (referred to E484Q) for B.1.617.1 (Kappa) and T22917A (referred to L452Q) and T23031C (ref
High diversity in Delta variant across countries revealed by genome-wide analysis of SARS-CoV-2 beyond the Spike protein.
Result: Within the Spike protein, there are four such mutations (T19R, L452R, T478K, and P681R) as well (mean prevalenceDelta = 99.86%, mean prevalenceotherVariantsofConcern = 0.04%).
Table: T478K
Figure: Residues corresponding to Spike protein mutations T19R, T478K, and P681R are missing from the structure of the Spike protein and hence not shown here.
Linked nosocomial COVID-19 outbreak in three facilities for people with intellectual and developmental disabilities due to SARS-CoV-2 variant B.1.1.519 with spike mutation T478K in the Netherlands.
Introduction: Spike mutation T478K lies within the interaction domain with the human receptor ACE2.
Introduction: Little information is available on the B.1.1.519 variant with spike mutation T478K which became dominant in Mexico over the course of a few months: in October 2020, 5% of sequenced specimens were reported to be B.1.1.519, whereas in February 2021, this percentage had increased to 87%.
Result: Since the B1.1.519 lineage harbors a few mutations of interest in the spike protein includ
Discussion: Increased infectiousness of the B.1.1.519 variant could explain the high prevalence in Mexico and rapid transmission in our linked outbreak and could be caused by the T478K mutation or P681H which is shared with the B.1.1.7 variant.
Long-term, infection-acquired immunity against the SARS-CoV-2 Delta variant in a hamster model.
Introduction: The Delta variant is characterized by the spike protein amino acid mutations T19R, D614G, and D950N along with a deletion of two amino acids in the N-terminal domain at positions 157-158, antigenic mutations in the receptor binding domain (L452R and T478K), and a P681R mutation at the S1-S2 furin cleavage site.
Structural and biochemical rationale for enhanced spike protein fitness in delta and kappa SARS-CoV-2 variants.
Introduction: The Delta variant contains a novel T478K mutation within the RBD - that is not present in previous variants of concern - with uncharacterised effect.
Result: Further, the Delta variant lysine substitution at position 478 (T478K) extends its positively charged sidechain towards an electronegative region on ACE2 (centred at position E87).
Result: Interestingly, we observed enhanced potency of ab1 for both Kappa and Delta variant spikes relative to wild-type, despite the presence of the Kappa
Discussion: Analysis of the electrostatic surface potential of the ACE2-bound Delta variant S protein is consistent with enhancements in electrostatic complementarity afforded by both the L452R and T478K mutations.
Divergent SARS-CoV-2 Omicron-reactive T and B cell responses in COVID-19 vaccine recipients.
Mutations in the receptor-binding domain of human SARS CoV-2 spike protein increases its affinity to bind human ACE-2 receptor.
PMID: 35109768
2022
Journal of biomolecular structure & dynamics
Abstract: Here, we use the crystal structure of the RBD in complex with ACE-2 available in the public domain and analyse the 250 ns molecular dynamics (MD) simulations of wild-type and mutants; K417N, K417T, N440K, N501Y, L452R, T478K, E484K and S494P.
Neutralizing antibody responses elicited by SARS-CoV-2 mRNA vaccination wane over time and are boosted by breakthrough infection.
PMID: 35166573
2022
Science translational medicine
Introduction: The recently emerged Delta (B.1.617.2) variant is characterized by additional NTD alterations together with crucial RBD mutations (L452R and T478K).
SARS_CoV_2 mutation literature information.
PMID: 
2022
ACS infectious diseases
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