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REVIEW article

Front. Virol.
Sec. Viral Disease Investigation
Volume 4 - 2024 | doi: 10.3389/fviro.2024.1405680

Investigation of COVID-19 virus mutagenicity and the effect of the NSP13, NSP14, and NSP16 on the -1 ribosomal frameshifting

Provisionally accepted
  • 1 Student research committee, Hamadan University of Medical Sciences, Hamadan University of Medical Sciences, Hamedan, Hamadan, Iran
  • 2 Department of Microbiology, School of Medicine, Hamadan University of Medical Sciences, Hamadan, Hamadan, Iran
  • 3 Department of Medical Microbiology, Faculty of Medicine, Hamadan University of Medical Sciences, Hamadan, Hamadan, Iran
  • 4 Department of Pharmaceutical Biotechnology, School of Pharmacy, Hamadan University of Medical Sciences, Hamadan, Iran
  • 5 Hamadan University of Medical Sciences, Hamedan, Iran

The final, formatted version of the article will be published soon.

    The COVID-19 virus is a single-stranded virus from the Coronaviridae family and has a genome of about 29881 bp, which causes acute respiratory disease. One way of transmission of the COVID-19 virus is respiratory, which is the reason for the significant transmission of the disease. The COVID-19 virus causes mutagenesis in different parts of the virus genome with its mechanisms, including -1 ribosomal frameshifting. Various parts that have undergone the most severe mutations include the spike protein, which leads to the emergence of new variants. Most of the mutations observed in the COVID-19 virus are located in the S protein and a region known as the RBD (Receptor-Binding Domain), which binds to the ACE2 (Angiotensin-converting enzyme 2) receptor in human cells. The variations in the RBD region will determine how it binds to the ACE2 receptor. Essentially, the changes created because of the mutation determine the affinity of the RBD to ACE2. On the other hand, the COVID-19 virus, because of its NSP13, NSP14, and NSP16 proteins, helps the mutation of the virus by consuming magnesium ions (Mg 2+ ). Since the ribosome is stable with Mg 2+ , the COVID-19 virus, by consuming Mg 2+ , 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 -1 ribosomal frameshifting.

    Keywords: COVID-19 virus, Proteins S (Spike), RBD, ACE2, -1 ribosomal frameshifting, Magnesium

    Received: 23 Mar 2024; Accepted: 10 Jun 2024.

    Copyright: © 2024 Khanifar, Taheri, nouri and hosseini. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Mohammad Taheri, Department of Medical Microbiology, Faculty of Medicine, Hamadan University of Medical Sciences, Hamadan, Hamadan, Iran

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.