SARS-CoV-2 testing and sequencing for international arrivals reveals significant cross border transmission of high risk variants into the United Kingdom.
Introduction: P681H is adjacent to the furin cleavage site, potentially affecting membrane fusion.
A Simple Reverse Transcriptase PCR Melting-Temperature Assay To Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.
PMID: 34288729
2021
Journal of clinical microbiology
Introduction: The B.1.1.7 variant has a number of mutations in the spike protein, including single-nucleotide polymorphisms (SNPs) resulting in N501Y, A570D, D614G, and P681H mutations and deletions at amino acids 69 and 70 and 144Y.
Ongoing global and regional adaptive evolution of SARS-CoV-2.
Figure: Black nodes correspond to key amino acid substitutions S L18F, S A222V, S S477N, S N501Y, S D614G, S P681H, S T716I, N R203K, and N G204R.
Trajectory of Growth of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Variants in Houston, Texas, January through May 2021, Based on 12,476 Genome Sequences.
PMID: 34303698
2021
The American journal of pathology
Result: Eighteen patients with this N440K replacement were identified, and 10 patients had the identical combination of spike amino acid replacements: L18R, T95I, R158S, N440K, D614G, P681H, A688V, S735A, and T1027I.
Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
Method: The B.1.1.7 Spike we used carries the mutations found in GISAID Accession Number EPI_ISL 668152: del 69-70, del145, N501Y, A570D, D614G, P681H, T716I, S982A, and D1118H.
Structural modelling of SARS-CoV-2 alpha variant (B.1.1.7) suggests enhanced furin binding and infectivity.
Introduction: Furthermore, to understand the stability of the S-protein P681H mutation, compared the S-protein B.1.1.7 variant upon interaction with furin, both states were subjected to 100ns molecular dynamic (MD) simulations.
Introduction: Hence, in this study, we compared the S-protein-B.1.1.7 variant structure in complex with furin with the S-protein P681H-furin complex to determine if the B.1.1.7 variant or the P681H mutation affected furin cleavage.
Introduction: In addition, we calculated the binding affinity of furin to S-protein-P681H and S-protein-B.1.1.7 variant using Generalized-Born surface area molecular mechanics (MM/GBSA).|
Conformational Variability Correlation Prediction of Transmissibility and Neutralization Escape Ability for Multiple Mutation SARS-CoV-2 Strains using SSSCPreds.
Result: B.1.1.7 and B.1.617.2 strains have the P681H/R mutation sites at the furin cleavage site of SARS-CoV-2.
Result: The sequence flexibility/rigidity map patterns of the P681H/R mutation sites are more flexible than that of the wild-type strain.
Figure: Sequence flexibility/rigidity maps of all of the single amino acidmutations at the P681H/R mutation sites (blue: identical alpha-helix-typeconformations; red: identical beta-sheet-type conformations; andgreen: identical other-type conformations).
Transformations, Lineage Comparisons, and Analysis of Down-to-Up Protomer States of Variants of the SARS-CoV-2 Prefusion Spike Protein, Including the UK Variant B.1.1.7.
SARS_CoV_2 mutation literature information.
PMID: 
2021
EClinicalMedicine
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