Discussion: Also, there were two other sequences sampled from Shiraz in January 2021, which had five specific mutations as indicator of the Alpha variant (D614G, H69del, N501Y, V70del, Y144del) and were clustered along with the Alpha variants in phylogenetic tree; however, these sequences did not contain the other specific mutations of Alpha variant including A570D, D1118H, L699I, P681H, S982A and T716I.
Emergence of a novel SARS-CoV-2 Pango lineage B.1.1.526 in West Bengal, India.
PMID: 34896696
2022
Journal of infection and public health
Introduction: Along with the clade specific mutations, these variants have their own sets of characteristics mutations including several mutations in the S glycoprotein like Delta69-70, Delta144-145, N501Y, A570D, P681H, T716I, S982A, D1118H in the Alpha variant; D80A,
Discussion: N501Y mutation, shared by the three VOCs Alpha, Beta and Gamma, could enhance the affinity of the S protein with ACE2, especially with the side chains of residues Y41 and K353 of ACE2 [27,].
Discussion: In addition, N501Y mutation enabled the virus to infect BALB/c mice, which expanded its host range.
Efficacy of mRNA, adenoviral vector, and perfusion protein COVID-19 vaccines.
Abstract: All strains other than the delta mutant are often found with the N501Y mutation situated on the RBD, resulting in higher binding between the spike protein and angiotensin-converting enzyme 2 (ACE2) receptors, enhanced viral adhesion, and following the entrance to host cells.
Introduction: Eight of these mutations are in the spike protein (S), including 69/70/144 deletion, N501Y, A570D, P681H, T716I, S982A, D1118H.
Introduction: Higher selectivity of the spike protein for ACE2 receptors is shown in
Table: N501Y
Omicron and Delta variant of SARS-CoV-2: A comparative computational study of spike protein.
Abstract: Based on docking studies, the Q493R, N501Y, S371L, S373P, S375F, Q498R, and T478K mutations contribute significantly to high binding affinity with human ACE2.
E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.
PMID: 34915409
2022
International immunopharmacology
Discussion: Data suggest that N501Y mutant RDB gains few pi-pi stacking and pi-cation interactions during antibody recognition which accounts for less reduction in binding affinity for this mutant with B38 mAB.
Discussion: In addition, N501Y mutant lose several additional hydrogen bonding interactions with the B38 mAB.
Discussion: Not only the interaction pattern, but also the N501Y mutation allows stabilization and close packing of the RBD with ACE2 interface.
Discussion: Previous modeling and simulation studies showed contradicting results for N501Y mutant on ACE2 recognition.
Discussion: Recent data suggest that N501Y mutation does not significantly alter the binding affinity with Bamlanivimab.
Discussion: recently evaluated the susceptibility
The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants.
Abstract: There is a major response to N501Y, including a public IgVH4-39 sequence, with E484K and K417N also targeted.
Abstract: Two of these RBD-binding mAbs recognize a neutralizing epitope conserved between SARS-CoV-1 and -2, while 18 target mutated residues in Beta: K417N, E484K, and N501Y.
Table: N501Y
Figure: (A-F) Neutralization assays performed against Victoria, Alpha (N501Y), Beta (K417N, E484K, and N501Y), Gamma (K417T, E484K, and N501Y
Omicron N501Y mutation among SARS-CoV-2 lineages: Insilico analysis of potent binding to tyrosine kinase and hypothetical repurposed medicine.
PMID: 34929375
2022
Travel medicine and infectious disease
Introduction: All the three variants retain N501Y mutation on spike protein receptor binding domain (RBD) which is required for binding to human receptor ACE2 (hACE2) for viral entry to host cells.
Introduction: However, not much are reported as an evidence of kinase or other signaling pathways resulting the severe complications or increased death rate by variant containing N501Y mutation has been concluded.
Introduction: The N501Y mutation localizes at RBD that
Introduction: The B.1.1.7 is reported to be more infectious with higher spreading rate and increased binding affinity to ACE2 in particular due to N501Y, compared with other mutations such as E484K.
Pierce into Structural Changes of Interactions Between Mutated Spike Glycoproteins and ACE2 to Evaluate Its Potential Biological and Therapeutic Consequences.
PMID: 34931119
2022
International journal of peptide research and therapeutics
Abstract: The obtained results revealed that the N501Y substitution has altered the interaction orientation, augmented the number of interface bonds, and increased the affinity against the ACE2.
Introduction: The first mutation is the N501Y that is one of the six central contact residues in the receptor-binding domain (RBD) of the spike protein.
Discussion: Identical binding energies for engineered-ACE2/wild-type-RBD and engineered-ACE2/mutant-RBD complexes reveal that any loss of stabilizing interaction, due to the N501Y substitution, is compensated with novel and equivalent interactions.
Discussion: The interactions between the engineered ACE2 and mutant spike protein showed that the
Enhanced fitness of SARS-CoV-2 variant of concern Alpha but not Beta.
Introduction: Beta has nine mutations in S, including N501Y, and two in the S receptor-binding domain (RBD), K417N and E484K.
Introduction: In contrast to hACE2-K18Tg mice, hACE2-KI mice show physiological expression of human ACE2, with no ectopic expression of human ACE2 in the brain, and no expression of mouse ACE2, which has been shown to be permissive to the spike mutation N501Y contained in SAlpha.
Introduction: Some of the S mutations, such as N501Y and the H69/V70 deletion, have been hypothesized to enhance replication and transmission, but there is a lack of clear experimental evidence for this.
Discussion: We have show
Genomic characterization of the dominating Beta, V2 variant carrying vaccinated (Oxford-AstraZeneca) and nonvaccinated COVID-19 patient samples in Bangladesh: A metagenomics and whole-genome approach.
Abstract: Noteworthily, the receptor binding domain (RBD) region of S protein of all the isolates harbored similar substitutions including K417N, E484K, and N501Y that signify the Beta, while D614G, D215G, D80A, A67V, L18F, and A701V substitutions were commonly found in the non-RBD region of Spike proteins.
SARS_CoV_2 mutation literature information.
PMID: 
2022
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