SARS_CoV_2 mutation literature information.


  The significant immune escape of pseudotyped SARS-CoV-2 variant Omicron.
 PMID: 34890524       2022       Emerging microbes & infections
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, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H,  PMID: 34896524       2022       Gene
Table: P681H
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
Discussion: Based on non-synonymous mutational analysis, here we revealed the emergence of a novel SARS-CoV-2 lineage B.1.1.526 harboring 11 coexisting mutations in seven different genes including D614G, P681H and V1230L in the S glycoprotein.
Discussion: Therefore, the novel lineage B.1.1.526 having D614G, P681H, V1230L and E484K mutations in the S glycoprotein is expected to have increased infectivity, high transmissibility, and enhanced immune evasion properties.
Discussion: Though the role of D614G in increased infectivity and transmissibility is well known, the functional relevance of P681H/R


  Structural and functional insights into the major mutations of SARS-CoV-2 Spike RBD and its interaction with human ACE2 receptor.
 PMID: 34955621       2022       Journal of King Saud University. Science
Introduction: Substitution mutations like D614G, N501Y, Y453F, N439K/R, P681H, K417N/T, and E484K, as well as deletion mutations like DeltaH69/V70 and Delta242-244 are the most common in the spike protein.


  A novel antibody against the furin cleavage site of SARS-CoV-2 spike protein: Effects on proteolytic cleavage and ACE2 binding.
 PMID: 35007661       2022       Immunology letters
Discussion: In contrast, the mutation of P681H (Alpha variant) and P681R (Delta variant) significantly increased viral replication and transmission, largely due to increased cleavage of S1/S2 site by furin enzyme.


  Emergence of two distinct variants of SARS-CoV-2 and an explosive second wave of COVID-19: the experience of a tertiary care hospital in Pune, India.
 PMID: 35000004       2022       Archives of virology
Result: Importantly, P681H was present in the UK variant B.1.1.7 (Table 2).
Discussion: It is pertinent to note here that a recent increase in COVID-19 cases in New York, USA, was observed to be due to the introduction of B.1.243 lineage strain with P681H and T478K mutations.
Discussion: The rapid global spread of the UK variant with P681H and P681R mutations is well known.


  Computational modelling of potentially emerging SARS-CoV-2 spike protein RBDs mutations with higher binding affinity towards ACE2: A structural modelling study.
 PMID: 34979405       2022       Computers in biology and medicine
Introduction: These variants, such as B.1.17 (Alpha variant) harbouring a mutation N501Y reported in the UK, D614G variant, lineage B.1.1.207 with P681H replacement, lineage B.1.351 (Beta) with E484K mutation reported in South Africa (B.1.351) and P.1 variant reported in Brazil.


  Isolation of SARS-CoV-2 B.1.1.28.2 (P2) variant and pathogenicity comparison with D614G variant in hamster model.
 PMID: 34959053       2022       Journal of infection and public health
Introduction: This variant has about 17 mutations, including N501Y, P681H, 69-70 deletion; the ORF8 Q27stop mutation outside the spike protein and is adapted to be more transmissible.


  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: On the other hand, the P681H mutation contributed to the increased cavity size and relatively higher residue depth.
Introduction: The third mutation, P681H, is located immediately near the furin cleavage site.
Result: According to the results of the multiple sequence alignment, the mutations of the EPI_ISL_601443 variant were as follows: H69 deletion, V70 deletion, Y144 deletion, N501Y substitution, A570D substitution, D614G substitution, P681H substitution, T716I substitution, S982A substitution, and D1118H substitution.

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