Acquiring insights through a sequence-based approach to the critical Zika virus MTase domain | [Advancements in life sciences • 2024]

Author(s):

1. Banan Atwah: Department of Clinical Laboratory Sciences, Faculty of Applied Medical Sciences, Umm Al-Qura University,Makkah - Kingdom of Saudi Arabia

2. Saad Alghamdi: Department of Clinical Laboratory Sciences, Faculty of Applied Medical Sciences, Umm Al-Qura University,Makkah - Kingdom of Saudi Arabia

3. Nizar H. Saeedi: Department of Medical Laboratory Technology, Faculty of Applied Medical Sciences, University of Tabuk,Tabuk - Kingdom of Saudi Arabia

4. Abdulrahman Alzahrani: Department of Applied Medical Sciences, Applied College, Al-Baha University, Al-Baha City , Kingdom of Saudi Arabia

5. Rashed Mohammed Alghamdi: Department of Laboratory Medicine, Faculty of Applied College, Al-Baha University , Kingdom of Saudi Arabia

6. Asif Hussain Akber: Department - Virology Division, Prince Sultan Military Medical City, Riyadh - Kingdom of Saudi Arabia

7. Mohammed Yahya Al Qahtani: Department - Virology Division, Prince Sultan Military Medical City, Riyadh - Kingdom of Saudi Arabia

8. Atiah Abkar Yahya Mujarribi: Department - Virology Division, Prince Sultan Military Medical City, Riyadh , Kingdom of Saudi Arabia

9. Saeed Saleh Al Qahtani: Department Microbiology Division, Prince Sultan Military Medical City, Riyadh ,Kingdom of Saudi Arabia

10. Ahmed Mohammed Faqihi: Department Microbiology Division, Prince Sultan Military Medical City, Riyadh ,Kingdom of Saudi Arabia

11. Mohammad Azhar Kamal: Department of Pharmaceutics, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Alkharj ,Kingdom of Saudi Arabia

Abstract:

Background: ZIKV is one of the re-emerging arboviruses (viruses carried by arthropods), which is spread through the Aedes mosquito. It is an RNA virus with only one strand that is appropriate to the family Flaviviridae's Flavivirus (genus) & has been linked to other Flaviviruses such as the West Nile virus, chikungunya virus, & dengue (DENV) virus. The envelope, precursor membrane, and capsid are three structural proteins, and seven nonstructural proteins are also encoded by the Zika virus genome. Methods: We conducted an in-silico analysis of the Zika virus' MTase domain protein for this publication. We predicted that methylation would play a significant role in the available Prosite, Pfam, and InterProScan tools to aid in locating the MTase domain. Along with alignment, amino acid composition, charged amino acids, atomic level studies, & molecular weight, we also make predictions for these variables, including theoretical Pi. Results: We also examine the MTase domain's simulated structure (alpha helix, beta sheet, turn) and its specifics, including secondary structure. We also pinpoint the locations where proteins, DNA, and RNA bind. Potential phosphorylation sites can be found on the Ser, Thr, and Tyr residues in the MTase domain. Conclusion: These outcomes imply a complicated interaction between different phosphorylation modifications that modulates the activity of the MTase domain. To fully appreciate the auxiliary and practical perspectives and to clarify the varied roles of PTM in the MTase domain will be a primary goal of future study.

Page(s): 430-437

DOI: DOI not available

Published: Journal: Advancements in life sciences, Volume: 11, Issue: 2, Year: 2024

Keywords:

Secondary structure , ITASSER , Prosite , ahelix Pfam , InterProScan , Binding sites , Posttranslationa modification , SOPMA Phyre2

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