|
Basic Characteristics of Mutations
|
|
Mutation Site
|
L452R |
|
Mutation Site Sentence
|
Examination of 1 048 576 nucleotide sequences from SARS‐CoV‐2 spike (S) glycoproteins revealed a total of 46 mutations. Annotation of the complete sequence of the S protein, consisting of 1273 amino acids (aa), delineated the S1‐domain as spanning aa 14‐685, in which five prevalent mutations were identified: aspartic acid 614 to glycine (D614G), leucine 452 to arginine (L452R), proline 681 to arginine (P681R), threonine 19 to arginine (T19R), and threonine 478 to lysine (T478K). |
|
Mutation Level
|
Amino acid level |
|
Mutation Type
|
Nonsynonymous substitution |
|
Gene/Protein/Region
|
S |
|
Standardized Encoding Gene
|
S
|
|
Genotype/Subtype
|
- |
|
Viral Reference
|
-
|
|
Functional Impact and Mechanisms
|
|
Disease
|
Cell line
|
|
Immune
|
- |
|
Target Gene
|
-
|
|
Clinical and Epidemiological Correlations
|
|
Clinical Information
|
- |
|
Treatment
|
- |
|
Location
|
- |
|
Literature Information
|
|
PMID
|
39535372
|
|
Title
|
Inactivation of Pseudovirus Expressing the D614G Spike Protein Mutation using Nitric Oxide-Plasma Activated Water
|
|
Author
|
Patel P,Kaushik N,Acharya TR,Lenka SS,Ghosh S,Wahab R,Verma SK,Choi EH,Kaushik NK
|
|
Journal
|
Advanced science (Weinheim, Baden-Wurttemberg, Germany)
|
|
Journal Info
|
2024 Dec;11(48):e2411515
|
|
Abstract
|
Variants of concern (VOCs) of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) exhibit high infectivity due to mutations, particularly in the spike protein, that facilitate enhanced binding of virus to human angiotensin-converting enzyme 2 (hACE2). The D614G mutation, situated in S1-domain, promotes the open conformation of spike protein, augmenting its interaction with hACE2. Activated water neutralizes pathogens by damaging biological molecules; however, its effect on mutated SARS-CoV-2 or VOCs requires further exploration. Here, the efficacy of nitric oxide (NO(x))-plasma activated water (PAW) in inhibiting infections by SARS-CoV-2 pseudovirus expressing D614G-mutated spike protein is investigated, which serves as a model for mutated SARS-CoV-2. Results demonstrated high prevalence of D614G mutation in SARS-CoV-2 and its VOCs. NO(x)-PAW is non-toxic to cells at high concentration, inhibiting infection by 71%. Moreover, NO(x)-PAW induced structural changes in S1-domain of spike protein, reducing its binding affinity and lowering clathrin-mediated endocytosis-related gene expression. Additionally, in silico analysis revealed NO(x) species in NO(x)-PAW played key role in impairing S1-domain function of the mutated SARS-CoV-2 pseudovirus by interacting directly with it. Collectively, these findings reveal the potent inactivation ability of PAW against mutated SARS-CoV-2 and suggest its potential application in combating emerging variants of SARS-CoV-2 and other viral threats.
|
|
Sequence Data
|
-
|
|
|