Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

V483a – an Emerging Mutation Hotspot of Sars-Cov-2

Version 1 : Received: 15 September 2020 / Approved: 17 September 2020 / Online: 17 September 2020 (10:43:02 CEST)

How to cite: Ashwaq, O.; Manickavasagam, P.; Haque, S.M. V483a – an Emerging Mutation Hotspot of Sars-Cov-2. Preprints 2020, 2020090395. Ashwaq, O.; Manickavasagam, P.; Haque, S.M. V483a – an Emerging Mutation Hotspot of Sars-Cov-2. Preprints 2020, 2020090395.


Exploring the biological significance of mutations in SARS-CoV-2 coronavirus, causing the COVID–19 pandemic, has recently become an area of paramount interest for many researchers, who are pouring their tremendous efforts, in cracking the COVID–19 pandemic code. One of many such mutations that have occurred in the viral genome is V483A mutation, which is a part of the receptor-binding motif (RBM), present in the S1 domain of the spike protein. V483A mutant virus is becoming popular in North America with 36 cases so far, due to its frequent occurrences in recent days. In this review, we 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 is made between the wild type and the V483A mutants to analyze certain factors like the 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. Comprehensive details about infectivity and evasion of the immune system by the virus are discussed. This information can in turn be of monumental importance in the field of vaccine and drug development because the mutants are becoming resistant to the vaccines and monoclonal antibodies.


Spike protein, V483A, substitution mutation, virus-host cell interaction, high transmission, infectivity.


Biology and Life Sciences, Virology

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