Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
PMID: 34123874
2021
Frontiers in cellular and infection microbiology
Figure: (A) Shows the alignment for the 69/70 deletion assay; (B) shows the alignment for the K417N mutation assay; (C) shows the alignment for the E484K/N501Y assay.
Figure: (A) The green curve shows the amplification of the probe directed to the sequence without the E484K mutation (FAM), while the signal by the probe directed to the sequence that presents the mutation remains without amplification signal; (B) the orange curve shows the amplification of the probe directed to the E484K mutation (CFR 610), while the probe directed to the sequence without mutation remains without amplification signal; (C) the blue curve shows the amplification of the probe directed to the sequence without mutation N501Y (HEX), while the probe directed to the sequence with the mutation remains without a
Rapidly emerging SARS-CoV-2 B.1.1.7 sub-lineage in the United States of America with spike protein D178H and membrane protein V70L mutations.
Abstract: It is defined by the N501Y mutation in the receptor-binding domain (RBD) of the Spike (S) protein, and a few other mutations.
Introduction: The Spike (S) protein N501Y mutation in the receptor-binding domain (RBD) confers higher binding affinity of the S protein for ACE2, while the other two deletions, HV69-70del and Y144del in the N-terminal domain (NTD) may also play a role in ACE2 receptor binding or neutralizing antibody escape.
Discussion: This is the same observed with other deleterious mutations like the N501Y and E484K
Rapid Increase of SARS-CoV-2 Variant B.1.1.7 Detected in Sewage Samples from England between October 2020 and January 2021.
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: Mutation N501Y, located within the receptor-binding domain (RBD), can increase binding affinity to human and murine angiotensin-converting enzyme 2 (ACE-2) receptor and cell infectivity in mice.|mg
Figure: (A) Deletion of nucleotides 21765 to 21770 (deletion of amino acids HV69-70); (B) deletion of nucleotides 21991 to 21993 (deletion of amino acid Y144); (C) mutation A23063T (amino acid change N501Y); (D) mutation C23271A (amino acid change A570D).
Rapid and simultaneous identification of three mutations by the Novaplex SARS-CoV-2 variants I assay kit.
Abstract: Of them, two harbored both H69/V70 deletion and N501Y substitution, whereas two harbored E484K substitution alone.
Introduction: All three VOCs listed above harbor the N501Y mutation; B.1.1.7 harbors an additional H69/V70 deletion; and the other two, the E484K substitution mutation.
Introduction: Among the various mutations emerging in SARS-CoV-2, those in the spike (S) protein, specifically the H69/V70 deletion and E484K N501Y substitution mutations, are important because the S protein is involved in infectivity to host cells via angiotensin-converting enzyme 2 and the main target of neutralizing antibodies induced by vaccines.
Discussion: In Japa
Proliferation of SARS-CoV-2 B.1.1.7 Variant in Pakistan-A Short Surveillance Account.
Abstract: Based on the partial sequencing of SGTF samples 93.5% (n = 29/31) showed the characteristic N501Y, A570D, P681H, and T716I mutations found in the B.1.1.7 variant.
Abstract: Several mutations have been reported in the genome of the B.1.1.7 variant including the N501Y and 69-70de
Table: N501Y
Figure: (B) District wise distribution of SGTF cases which are sequenced and having N501Y mutation.
Discussion: The sequencing results confirmed 93% (n = 29/31) cases as B.1.1.7, having the marker S protein mutations (N501Y, A570D, P681H, and T716I).
Quantitative analysis of ACE2 binding to coronavirus spike proteins: SARS-CoV-2 vs. SARS-CoV and RaTG13.
PMID: 34137759
2021
Physical chemistry chemical physics
Abstract: Both calculations confirmed a significant increase of the binding affinity of the N501Y mutant to ACE2 and explained its molecular mechanism.
Abstract: We also calculated an important mutation of N501Y in SARS-CoV-2 using both alanine scanning calculation and a thermodynamic integration (TI) method.
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).
Introduction: Previous studies suggest that both the E484K and N501Y mutations in the RBD may enhance the binding affinity of the S protein for hACE2.
Result: However, studies have shown that the N501Y mutation in the RBD renders mice susceptible to SARS-CoV-2 infection.
Result: Taken together, these observation
An ACE2 Triple Decoy that neutralizes SARS-CoV-2 shows enhanced affinity for virus variants.
5Result: All but the construct expressing L452R/K417N showed higher affinity for ACE(WT) (Table S7 in the ""Supplementary Information S1""), which aligns with what might be predicted from the results in Table S5:K417N decreases affinity and N501Y increases affinity."
Result: 3s, inhibition in the surrogate virus neutralization assay modified to assess competition by the ACE2 Triple Decoy for ACE2 (WT) binding to S RBD was similar for S RBD WT, E484K, N501Y, L452R, and K417N/E484K/N501Y.
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: Among the mutations in the B.1.1.7, nine mutations, including H69-V70 deletion (Delta69/Delta70), Y144 deletion (Delta144), N501Y, A570D, D614G, P681H, T716I, S982A, and D11
Rational optimization of a human neutralizing antibody of SARS-CoV-2.
PMID: 34147856
2021
Computers in biology and medicine
Introduction:
Introduction: Experimental data suggests mutation N501Y increases the binding affinity of the spike protein with human and murine ACE2.
Introduction: It is estimated that the spread of SARS-CoV-2 N501Y variant is 70% faster than previous strains, indicating a much higher infectivity.
Introduction: N501 of RBD is spatially distant from its interacting interface with P2B-2F6, and thereby the newly identified mutation N501Y is unlikely to affect the neutralizing activity of P2B-2F6.
Introduction: These variants have an unusually large number of genetic changes, including the noteworthy spike protein mutation N501Y, one of the key residues in RBD domain interacting with ACE2.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Frontiers in cellular and infection microbiology
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