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Analysis of predicted proteasomal cleavages in the methyltransferase domain from JEV


Sarah Afaq1,*, Arshi Malik2, Md. Salman Akhtar3, Afaf S. Alwabli4, Dhafer A. Alzahrani5, Habeeb M. Al-Solami6, Othman Alzahrani7, Qamre Alam8, Mohammad Azhar Kamal9,10, Aala A. Abulfaraj11



1,2Department of Clinical Biochemistry, College of Medicine, King Khalid University, Abha, Kingdom of Saudi Arabia; 3Department of Basic Medical Sciences, Faculty of Applied Medical Sciences, Al-Baha University, Al-Baha, Kingdom of Saudi Arabia; 4,5,6Department of Biological Sciences, Faculty of Science, King Abdulaziz University, Jeddah 21589, Kingdom of Saudi Arabia; 7Department of Biology, Faculty of Science, University of Tabuk, Tabuk, Kingdom of Saudi Arabia; 8Medical Genomics Research Department, King Abdullah International Medical Research Center, King Saud bin Abdulaziz University for Health Sciences, Ministry of National Guard Health Affairs, Riyadh, Saudi Arabia; 9Department of Biochemistry, Faculty of Science, University of Jeddah, Jeddah, Saudi Arabia; 10University of Jeddah Center for Science and Medical Research (UJC-SMR), Jeddah, Saudi Arabia; 11Department of Biology, Science and Arts College, Rabigh Campus, King Abdulaziz University, Jeddah, Saudi Arabia; Dr. Sarah Afaq - Email: safaq@kku.edu.sa; Department of Clinical Biochemistry, College of Medicine, King Khalid University, Abha Kingdom of Saudi Arabia, PO Box 641; *Corresponding author



Author contacts: Arshi Malik - E-mail: amalik@kku.edu.sa; Md. Salman Akhtar - E-mail: milyas@bu.edu.sa; Afaf S. Alwabli - E-mail: aalwabili@stu.kau.edu.sa; Dhafer A. Alzahrani - E-mail: dalzahrani@kau.edu.sa; Habeeb M. Al-Solami - E-mail: hmalsolami@kau.edu.sa
Othman Alzahrani - E-mail: o-alzahrani@ut.edu.sa; Qamre Alam - E-mail: alamqa@ngha.med.sa; Mohammad Azhar Kama - E-mail: maksmal@uj.edu.sa; Aala A. Abulfaraj - E-mail: aaabulfaraj@kau.edu.sa Submitted by Dr. Mohammad Tarique, Center for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi-110025, India; E-mail id: tariqueaiims@gmail.com


Article Type

Research Article



Received September 22, 2019; Revised February 15, 2020, Accepted February 20, 2020; Published March 31, 2020



The methyltransferase (MTase, a 265 amino acid residues long region at the N-terminal end of the viral nonfunctional supermolecule NS5 domain) is key for viral replication in Japanese Encephalitis Virus (JEV). Sequence to structure to functional information with adequate knowledge on MTase from JEV is currently limited. Therefore, it is of interest to document a report on the comprehensive analysis of predicted proteasomal cleavage data in the methyltransferase domain from JEV. This data is relevant in the design and development of vaccine and other therapeutic candidates for further consideration.



Japanese encephalitis (JEV), infection, methyltransferase, proteasome, cleavage



Afaq et al. 16(3): 223-228 (2020) 


Edited by

P Kangueane






Biomedical Informatics



This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.