An in-silico analysis of OGT gene association with diabetes mellitus

Article


Ayodele, O., Udosen, B., Oluwagbemi, O., Oladipo, E., Omotuyi, I., Isewon, I., Nash, O., Soremekun, O. and Fatumo, F. 2024. An in-silico analysis of OGT gene association with diabetes mellitus. BMC Research Notes. 17. https://doi.org/10.1186/s13104-024-06744-5
TypeArticle
TitleAn in-silico analysis of OGT gene association with diabetes mellitus
AuthorsAyodele, O., Udosen, B., Oluwagbemi, O., Oladipo, E., Omotuyi, I., Isewon, I., Nash, O., Soremekun, O. and Fatumo, F.
Abstract

O-GlcNAcylation is a nutrient-sensing post-translational modification process. This cycling process involves two primary proteins: the O-linked N-acetylglucosamine transferase (OGT) catalysing the addition, and the glycoside hydrolase OGA (O-GlcNAcase) catalysing the removal of the O-GlCNAc moiety on nucleocytoplasmic proteins. This process is necessary for various critical cellular functions. The O-linked N-acetylglucosamine transferase (OGT) gene produces the OGT protein. Several studies have shown the overexpression of this protein to have biological implications in metabolic diseases like cancer and diabetes mellitus (DM). This study retrieved 159 SNPs with clinical significance from the SNPs database. We probed the functional effects, stability profile, and evolutionary conservation of these to determine their fit for this research. We then identified 7 SNPs (G103R, N196K, Y228H, R250C, G341V, L367F, and C845S) with predicted deleterious effects across the four tools used (PhD-SNPs, SNPs&Go, PROVEAN, and PolyPhen2). Proceeding with this, we used ROBETTA, a homology modelling tool, to model the proteins with these point mutations and carried out a structural bioinformatics method– molecular docking– using the Glide model of the Schrodinger Maestro suite. We used a previously reported inhibitor of OGT, OSMI-1, as the ligand for these mutated protein models. As a result, very good binding affinities and interactions were observed between this ligand and the active site residues within 4Å of OGT. We conclude that these mutation points may be used for further downstream analysis as drug targets for treating diabetes mellitus.

KeywordsSingle nucleotide polymorphism (SNPs); O-linked N-acetylglucosamine transferase (OGT), 3 and 4
Sustainable Development Goals3 Good health and well-being
Middlesex University ThemeHealth & Wellbeing
PublisherBioMed Central
JournalBMC Research Notes
ISSN
Electronic1756-0500
Publication dates
Online27 Mar 2024
Publication process dates
Submitted15 Jun 2023
Accepted08 Mar 2024
Deposited10 Apr 2024
Output statusPublished
Publisher's version
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File Access Level
Open
Copyright Statement

This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

Digital Object Identifier (DOI)https://doi.org/10.1186/s13104-024-06744-5
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