The D614G mutations in the SARS-CoV-2 spike protein: Implications for viral infectivity, disease severity and vaccine design.
PMID: 33199022
2021
Biochemical and biophysical research communications
Introduction: However, antigenic drift is known to occur among the endemic human coronaviruses, and during the first SARS outbreak in 2003, a single amino acid mutation in SARS-CoV (D480 A/G) within the receptor binding domain (RBD) of the Spike (S) protein became the dominant variant due to its ability to escape from neutralising antibodies.
Structural Modeling of the SARS-CoV-2 Spike/Human ACE2 Complex Interface can Identify High-Affinity Variants Associated with Increased Transmissibility.
Result: We consider seven cases representing distinct animal-human adaptive mutations in the SARS-CoV S-protein (Figure 2 (a)): adaptations from civet, an intermediate animal host, to human ACE2 (Y442F, L472F); mutations obtained by reversing civet to human adaptations (L472P, N479K, D480G); unfavorable mutation (T487S); and a previously designed double mutant (Y442F/L472F) optimized for hACE2 binding.
Figure: Mutations L472F, L472P and Y442F/L472F produced local conformational distortions at the interaction interface (S-cyan, hACE2-gree
Implications of the Novel Mutations in the SARS-CoV-2 Genome for Transmission, Disease Severity, and the Vaccine Development.
Introduction: D480A/G variant has been shown to escape neutralizing antibody and immune pressure.
Introduction: In RBD of the spike protein, D480A/G mutation has emerged in patients with SARS-CoV infection and has become the dominant variant among 2003/2004 viruses.
Emerging mutation in SARS-CoV-2 spike: Widening distribution over time in different geographic areas.
Introduction: For example, the P462L and D480 A/G mutations that occur in SARS-CoV induce viruses to escape to a monoclonal NAb.
Crucial Mutations of Spike Protein on SARS-CoV-2 Evolved to Variant Strains Escaping Neutralization of Convalescent Plasmas and RBD-Specific Monoclonal Antibodies.
Introduction: During the SARS epidemic in 2003, the single amino acid mutation D480A/G in the RBD domain of SARS-CoV spike protein gradually became dominant, and subsequent study confirmed that this mutation occurred in a critical site and enabled the mutant escaping neutralizing antibodies.
Computational Saturation Mutagenesis of SARS-CoV-1 Spike Glycoprotein: Stability, Binding Affinity, and Comparison With SARS-CoV-2.
PMID: 34957216
2021
Frontiers in molecular biosciences
Table: D480G
Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus.
Introduction: D480A/G escapes neutralizing antibody 80R, and immune pressure from 80R in vitro could recapitulate emergence of the D480 mutation.
Introduction: Notably, a single SARS-CoV-1 amino acid change, Spike D480A/G in the receptor binding domain (RBD), arose in infected humans and civets and became the dominant variant among 2003/2004 viruses.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Biochemical and biophysical research communications
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