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Source: V483G Mutation  Sep 21, 2020  3 years, 6 months, 3 weeks, 6 days, 13 hours, 5 minutes ago

V483G Mutation: Warning About Growing Prevalence Of New SARS-CoV-2 Mutant Strain V483G That Is Antibody Resistant And Even More Infectious

V483G Mutation: Warning About Growing Prevalence Of New SARS-CoV-2 Mutant Strain V483G That Is Antibody Resistant And Even More Infectious
Source: V483G Mutation  Sep 21, 2020  3 years, 6 months, 3 weeks, 6 days, 13 hours, 5 minutes ago
V483G Mutation: Researchers And health Officials are warning that  that a mutant strain of the SARS-CoV-2 coronavirus, the V483G strain is fast making appearances in various countries including India, Brazil, The Middles-East, UK and even in the United States.


 
According to genomic experts and immunologist, the V483 strain is resistant to the neutralizing properties of antibodies and is also deemed to be even more infectious than the D614G strains.
 
In a new study by researchers from Saudia Arabia and India, the details of this new mutation was highlighted in the published findings on a preprint server and is pending peer review. https://www.preprints.org/manuscript/202009.0395/v1
 
Of the various emerging mutated strains, a mutation that is worrying and concerning that have occurred in the viral genome is the V483A mutation, which is a part of the receptor binding motif (RBM), present in the S1 domain of the spike protein. https://www.biorxiv.org/content/10.1101/2020.04.29.069054v1.full.pdf
 
This V483A mutant virus is becoming popular in North America with 36 cases detected in random sequencing studies recently so far and considering that many sequencing studies have not been conducted, its prevalence could be far more extensive.
 
In this study review, the team have assembled all information, currently available on V483A mutation, and have made a critical analysis based on the perspectives of many researchers all around the world.
 
Comparison was made between the wild type and the V483A mutants to analyze certain factors like type of interaction between the virus and host cell interface, binding affinity, stability, partition energy, hydrophobicity, occurrence rate, and transmissibility.
 
Insilico dynamic analysis shows minimal alteration in the receptor binding domain (RBD) of V483A mutant protein in free-state and no significant change of mutant tertiary structure of RBM upon binding to the ACE2 receptor.
 
The study findings