Introduction: Previous studies illustrated that D614G reduces the binding affinity to ACE2 but enhances the protease cleavage of S1/S2, leading to higher transmissibility.
Introduction: Specifically, BA.1 and BA.2 display 20 identical spike mutations, which are G339D, S373P, S375F, K417N, N440K, S477N, T478K, E484A, Q493R, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P68
Conformational dynamics and allosteric modulation of the SARS-CoV-2 spike.
Introduction: At the same time, the enhanced exposure of the RBM in the D614G variant led to increased sensitivity to neutralizing antibodies.
Introduction: By the summer of 2020, the SARS-CoV-2 S variant D614G (B.1 lineage) had supplanted the ancestral virus (strain Wuhan-1) worldwide, and structural analysis showed that D614G disrupts an interprotomer contact.
Introduction: Nonetheless, antibodies that target the S2 stalk further promoted the RBD-up conformation on the D614G spike.
Introduction: The D614G spike existed in an equilibrium where the RBD favors the up conformation prior to antibody binding.
Discu
Coronavirus Genomes and Unique Mutations in Structural and Non-Structural Proteins in Pakistani SARS-CoV-2 Delta Variants during the Fourth Wave of the Pandemic.
Result: The most common non-synonymous and indel mutations, present in all complete genome samples were spike_T478K, spike_T19R, spike_L452R, spike_F157del, spike_E156G, spike_P681R, spike_D614G, spike_R158del, and spike_G142D (Table 3).
Neutralisation Hierarchy of SARS-CoV-2 Variants of Concern Using Standardised, Quantitative Neutralisation Assays Reveals a Correlation With Disease Severity; Towards Deciphering Protective Antibody Thresholds.
Introduction: As the pandemic progressed, a number of single amino acid mutations in the Spike protein were detected, such as D614G and A222V.
Introduction: Referred to as Cluster 5 or B.1.1.298, several different groups of mutations were identified, with the most abundant population containing missense and deletion mutations on the Spike; 69/70del, Y453F and D614G.
Introduction: The D614G mutation was found to increase the density of Spike protein on virions and infectivity.
Table: D614G
Functional analysis of polymorphisms at the S1/S2 site of SARS-CoV-2 spike protein.
3Introduction: The D614G exchange increases the percentage of S proteins present in the ""open"" conformation required for efficient ACE2 binding and viruses bearing this exchange show accelerated transmission kinetics in animal models."
Introduction: Nevertheless, mutations in SARS-CoV-2 have been detected and viruses with a D614G exchange became dominant early in the pandemic.
Discussion: Why mutant S686G showed enhanced interaction with ACE2 is at present unclear but might be due to its RBD adopting a conformation that may favour ACE2 binding, which would be a similar effect as reported for mutation D614G that is also located outside of the RBD.
Circulation of SARS-CoV-2 Variants among Children from November 2020 to January 2022 in Trieste (Italy).
Abstract: The D614G amino acid substitution was detected in all isolated and amplified viral strains.
Result: Briefly, in all sequences (32/32, 100%), the D614G substitution was detected, lineage B.1.
Result: Finally, 1/32 sequence was the Omicron strain, with the followin
Discussion: In contrast, we did not find any differences in the viral load between the N439K and D614G strains.
Discussion: In our cohort, and compared to the D614G strain, the S477N viral load was slightly lower, while no difference in the clinical presentation was observed.
Discussion: The B.1 strain shows the D614G substitution, able to confer moderate advantages in viral infectiveness and transmissibility, compared to the Wuhan-Hu-1 strain.
Delta Variant with P681R Critical Mutation Revealed by Ultra-Large Atomic-Scale Ab Initio Simulation: Implications for the Fundamentals of Biomolecular Interactions.
Abstract: Here, using ultra large-scale ab initio computational modeling, we study the P681R and D614G mutations in the SD2-FP domain, including the effect of double mutation, and compare the results with the wild type.
Abstract: Together with the earlier reported mutation D614G in the same domain, it offers an excellent instance to investigate the nature of mutations and how they affect the interatomic interactions in the spike protein.
Result: Table S2 lists the structure information from VASP optimization for the four SD2-FP models in the Delta variant: (a) wild type (WT), (b) mutated P681R (R681), (c) mutated D614G (G614), and (d) double mutation (DM) labeled as G614-R681.
Discussion: In addition to these intra-protomer interactions, it has been structurally demo
Result: All SARS-CoV-2 genomes detected showed that the virus belonged to the clade 20A.EU2, with the presence of the characteristic S477N and the D614G mutations on the spike protein.
Discussion: The difference in D614G physicochemical properties has a significant impact on the three-dimensional structure of the spike protein, giving the RBD (Receptor Binding Domain) a more open conformation than the wild type strain (Wuhan-Hu-1) and, therefore, an improvement in virus interaction with the host's cell receptors.
Discussion: The major impact of such changes has already been described for the D614G mutation in which a polar, negatively charged aspartic acid (D) with a higher MW (114 g/mol) is substituted
Protective Immunity of the Primary SARS-CoV-2 Infection Reduces Disease Severity Post Re-Infection with Delta Variants in Syrian Hamsters.
Method: Delta AY.1 variant had D614G, E156G, F157del, K417N, L452R, P681R, R158del, T19R, T95I and T478K substitutions; the Delta variant had A222V, D614G, D950N, G142D, L452R,
Discussion: Comparable cell entry efficiency was reported by a recent study for the Delta sub-lineages with K417N mutation in comparison with the wildtype SARS-CoV-2 with the D614G mutation.
E-Volve: understanding the impact of mutations in SARS-CoV-2 variants spike protein on antibodies and ACE2 affinity through patterns of chemical interactions at protein interfaces.
Introduction: The Beta variant has non-synonymous spike mutations such as LAL 242-244 deletion, D80A, D215G, E484K, N501Y, A701V, L18F, R246I, K417N, and D614G.
SARS_CoV_2 mutation literature information.
PMID: 
2022
MedComm
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