Title : Investigation of COVID-19 virus mutagenicity and the effect of the NSP13, NSP14 and NSP16 on the -1 ribosomal frameshifting
The COVID-19 pathogen is a pathogen with a single strand of genetic material, belonging to the family coronaviridae. It possesses a genome that is approximately 29881 bp long, which results in the development of a respiratory disease with sudden onset. One of how the COVID-19 virus is transmitted is through the respiratory system, which accounts for the significant spread of the disease. The COVID-19 virus induces changes in different regions of its genetic material, employing mechanisms such as -1 ribosomal frameshifting. The spike protein, which undergoes the most pronounced mutations, plays a crucial role in the emergence of new variants. The majority of mutations observed in the COVID-19 virus have been reported in the S protein and a specific area known as the RBD. The RBD establishes a connection with the ACE2 receptor found in human cells. Changes in the RBD region will determine how it binds to the ACE2 receptor, in other words, the changes created as a result of the mutation determine the affinity of the RBD to ACE2. On the other hand, the presence of the NSP13, NSP14, and NSP16 proteins in the COVID-19 virus helps the mutation of the virus by consuming magnesium ions. Since the ribosome is stable with magnesium ions, the COVID-19 virus, by consuming magnesium ions, causes the ribosome to convert from the polysome to the monosome state, which causes a break in translation and finally leads to the formation of ribosomal -1 frameshifting.