Introduction: Amino acid substitutions at residue 417, K417N in B.1.351 and K417T in P.1, appear to improve evasion from antibodies in combination with N501Y and E484K.
Introduction: B.1.351 and P.1 variants have two more spike mutations of biological significance: E484K and K417N/T, both located in the RBD and both important for ACE-2 binding and antibody recognition.
Characterization of a new SARS-CoV-2 variant that emerged in Brazil.
Introduction: S protein plays a key role in viral binding to host cell receptors (i.e., human angiotensin-converting enzyme 2 [hACE2]), and the P.1 variant has three mutations (K417T, E484K, and N501Y) in the receptor-binding domain (RBD).
Recent progress on the mutations of SARS-CoV-2 spike protein and suggestions for prevention and controlling of the pandemic.
PMID: 34146731
2021
Infection, genetics and evolution
Abstract: Among these mutations, the most representative ones are substitution mutations such as D614G, N501Y, Y453F, N439K/R, P681H, K417N/T, and E484K, and deletion mutations of DeltaH69/V70 and Delta242-244, which confer the virus with enhanced infectivity, transmissibility, and resistance to neutralization.
Introduction: The most representative ones in the spike protein are substitution mutations such as D614G, N501Y, Y453F, N439K/R, P681H, K417N/T, and
Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.
Abstract: Of 9 single RBD mutants evaluated, K417T, E484K, and N501Y disrupted binding of 65% of the NAbs evaluated, consistent with the assignment of the SARS-CoV-2 P.1 Japan/Brazil strain as a variant of concern (VoC).
Introduction: Of the nine RBD variants tested, N501Y, E484K, and K417T disrupted binding to 65% of the NAbs evaluated.
Result: Based on the in silico NAb epitope analysis, nine
Figure: The horizontal red line highlights the RBD variants (K417T, E484K, and N501Y) that disrupt the binding of the largest number of NAbs.
Preliminary Structural Data Revealed That the SARS-CoV-2 B.1.617 Variant's RBD Binds to ACE2 Receptor Stronger Than the Wild Type to Enhance the Infectivity.
Introduction: These mutations in this strain may enhance virus transmissibility and infectivity, including the deletion of residues 69-70 and 144 and the substitution of A570D, D614G, T716I, S982A, D1118H, P681H, K417N, K417T, E484 K and N501Y.
Allosteric Cross-Talk among Spike's Receptor-Binding Domain Mutations of the SARS-CoV-2 South African Variant Triggers an Effective Hijacking of Human Cell Receptor.
PMID: 34161095
2021
The journal of physical chemistry letters
Introduction: In this scenario, it is tempting to argue that the BR variant, differing from the SA one only by the K417T@RBD substitution, may exploit the same strategy to foster viral propagation.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Nature
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