SARS_CoV_2 mutation literature information.


  The Spike of Concern-The Novel Variants of SARS-CoV-2.
 PMID: 34071984       2021       Viruses
Introduction: Although the P681H mutation at the furin cleavage site initially raised much interest, it has no significant impact on viral fitness and was only found to slightly increase S1/S2 cleavage in cell culture.


  Molecular epidemiology of SARS-CoV-2 isolated from COVID-19 family clusters.
 PMID: 34074255       2021       BMC medical genomics
Discussion: B.1.1.7 variant (multiple spike protein mutations: deletion 69-70, deletion 144, N501Y, A570D, D614G, P681H, T716I, S982A, D1118H).


  Epitope-specific antibody responses differentiate COVID-19 outcomes and variants of concern.
 PMID: 34081630       2021       JCI insight
Discussion: Besides the RBD, a P681H mutation located in the S1/S2 linker region of the spike has been detected in multiple VOCs.
Discussion: Nevertheless, we note that the P681H and S235F mutations only affected a few individuals in the cohort of patients examined herein while the majority of patients displayed no apparent antibody responses against the corresponding epitopes.
Discussion: We found that the P681H mutation in the spike and the S235F in the nucleocapsid rendered the corresponding epitopes completely incapable of binding antibodies generated against the original virus.


  SARS-CoV-2 Brazil variants in Latin America: More serious research urgently needed on public health and vaccine protection.
 PMID: 34109031       2021       Annals of medicine and surgery (2012)
Introduction: Other considerable modifications are A570D, D614G, P681H, 144Y deletion, and 69/70 deletion.


  Rapid Increase of SARS-CoV-2 Variant B.1.1.7 Detected in Sewage Samples from England between October 2020 and January 2021.
 PMID: 34128696       2021       mSystems
Introduction: Substitution P681H is immediately adjacent to the furin cleavage site, important for viral pathogenesis, whereas deletion of amino acids 69 and 70 has been identified in multiple lineages associated with different RBD mutations and has been related to the evasion to human immune response.


  Proliferation of SARS-CoV-2 B.1.1.7 Variant in Pakistan-A Short Surveillance Account.
 PMID: 34136461       2021       Frontiers in public health
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.
Introduction: The B.1.1.7 harbors 17 amino acid changes mostly in the Spike (S) protein (69-70del, 144del, N501Y, A570D, P681H, T716I, S982A, and D1118H).
Result: Based on the partial sequencing of spike gene of SGTF samples, 93.5% (n = 29/31) showed the characteristic N501Y,  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


  Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.
 PMID: 34149735       2021       Frontiers in immunology
Discussion: If increased ACE2 affinity is required for increasing viral infectivity, other mutations in the SARS-CoV-2 S, such as D614G, P681H, or several other changes, alone or together, must be responsible for enhanced ACE2 binding affinity.


  Tracking SARS-CoV-2 Spike Protein Mutations in the United States (2020/01 - 2021/03) Using a Statistical Learning Strategy.
 PMID: 34159336       2021       bioRxiv
Result: It is natural to name the haplotype T478K-D614G-P681H-T732A as a B.1.1.222.
Result: The P681H mutation occurs in the S1/S2 cleavage segment of the Spike protein, which is typically not resolved in cryo-electron microscopy or x-ray diffraction experiments.


  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.
 PMID: 34160124       2021       Chembiochem
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.



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