SARS_CoV_2 mutation literature information.


  The significant immune escape of pseudotyped SARS-CoV-2 variant Omicron.
 PMID: 34890524       2022       Emerging microbes & infections
Introduction: These mutations cover almost all the key mutations of the previous VOCs (Alpha, Beta, Gamma, and Delta), including K417N, E484A, and N501Y and other known mutations which are proved to change the sensitivity of the virus to neutralization by protective antibodies.
Result: There are 32 mutations on the Spike of Omicron, including the following sites: A67V, H69del-V70del, T95I, G142D-V143del-Y144del-Y145del, N211del-L212I, ins214EPE, G339D, S371L, S373P, S375F, K417N, N440K,


  Rapid and accurate detection of SARS-CoV-2 mutations using a Cas12a-based sensing platform.
 PMID: 34894625       2022       Biosensors & bioelectronics
Result: 4C and D), higher than observed for N501Y detection and in a previous study.
Result: Because CRISPR/Cas12a has been reported to differentiate SNPs with single-base resolution, we used Cas12a to identify SARS-CoV-2 N501Y, D614G, and 69/70 deletion mutations; these are the key mutations of SARS-CoV-2 VOC (Table S1).
Result: Furthermore, five samples carrying the N501Y mutation and two samples carrying the 69/70 deletion were identified.


  A comprehensive overview of identified mutations in SARS CoV-2 spike glycoprotein among Iranian patients.
 PMID: 34896524       2022       Gene
Table: N501Y
Discussion: L452R, T478K, N501Y and
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.
 PMID: 34906769       2022       Biomedicine & pharmacotherapy
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


  Omicron and Delta variant of SARS-CoV-2: A comparative computational study of spike protein.
 PMID: 34914115       2022       Journal of medical virology
Abstract: Based on docking studies, the Q493R, N501Y, S371L, S373P, S375F, Q498R, and T478K mutations contribute significantly to high binding affinity with human ACE2.


  Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
 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.


  The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants.
 PMID: 34921776       2022       Cell host & microbe
Introduction: The RBD mutations found in Alpha (N501Y), Beta (K417N, E484K, and N501Y), Gamma (K417T, E484K, and N501Y), and Delta (L452R and T478K) are lo
Introduction: The majority of potent mAbs are directed to the mutations present in the Beta RBD, principally N501Y, and E484K, underscoring the small antigenic distance between Beta and Gamma, the larger distance between early pandemic strains and Beta, and interestingly, few anti-Beta mAbs can neutralize Delta, consistent with the extreme antigenic distance between Beta and Delta.


  Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
 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 B.1.1.7 is reported to be more infectious with higher spreading rate and increased binding affinity to ACE2 in particular due to


  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.
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 N501Y<



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