Browsing by Author "Bella-Omunagbe, Mercy"

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Global research landscape of telomere biology in infectious diseases: mechanistic links between host–pathogen interactions and immune ageing
(Frontiers in Aging, 2026) Wakai, Theophilus N.; Yensii, Nina Ghislaine; Kernyuy, Fabrice Banadzem; Bella-Omunagbe, Mercy; Chinedu, Shalom Nwodo; Afolabi, Sunmola
Telomeres, nucleoprotein structures located at the ends of chromosomes, maintain genomic stability and regulate cellular lifespan, particularly in immune cells. Telomere shortening, driven by cell division and limited telomerase activity, accelerates immune ageing and increases susceptibility to infectious diseases. Chronic infections like HIV and tuberculosis exacerbate telomere attrition through sustained immune activation and oxidative stress. This study presents a bibliometric review of research on telomere length and infectious diseases from 2005 to 2025. Data from the Web of Science Core Collection were analysed using VOSviewer and CiteSpace, software tools for visualising co-authorship, citation, and keyword networks, to assess publication trends, collaborations, and themes. A total of 123 publications were identified, showing steady growth with a 60% increase in publications from 2020 to 2022 during the COVID-19 pandemic. Leading journals included Frontiers in Immunology, PLoS ONE, and Scientific Reports. The United States produced the largest share of publications, followed by Canada and Spain, with notable contributions from the University of British Columbia and Université de Montréal. Influential authors such as Côté HCF, Pick N, and Maan EJ have advanced research, particularly in the areas of HIV and tuberculosis. Keyword analysis highlighted two dominant themes: immune ageing and infection-related stress. Malaria research was comparatively scarce, underscoring a gap for future investigation. These findings inform future research on telomere-targeted interventions and epidemiological studies aimed at enhancing infectious disease management. This review provides a comprehensive overview of the field’s progress and identifies key areas for future investigation.
Molecular Docking Appraisal of Pleurotus ostreatus Phytochemicals as Potential Inhibitors of PI3K/Akt Pathway for Breast Cancer Treatment
(Bioinformatics and Biology Insights Volume 19:, 2025) Effiong, Magdalene Eno; Bella-Omunagbe, Mercy; Afolabi, Israel Sunmola; Chinedu, Shalom Nwodo
InTRoDuCTIon: Breast cancer (BC) is a heterogeneous disease involving a network of numerous extracellular signal transduction path ways. The phosphoinositide 3-kinase (PI3K)/serine/threonine kinase (Akt)/mechanistic target of rapamycin (mTOR) pathway is crucial for understanding the BC development. Phosphoinositide 3-kinase, phosphatase and tensin homolog (PTEN), mTOR, Akt, 3-phosphoinositide dependent kinase 1 (PDK1), FoxO1, glycogen synthase kinase 3 (GSK-3), mouse double minute 2 (MDM2), H-Ras, and proapoptotic B-cell lymphoma 2 (BCL-2) family protein (BAD) proteins are key drivers of this pathway and potential therapeutic targets. Pleurotus ostreatus is an edible mushroom that is rich in flavonoids and phenols that can serve as potential inhibitors of proteins in the PI3K/Akt/mTOR pathway. AIM: This study evaluated the anticancer properties of P ostreatus through a structure-based virtual screening of 22 biologically active com pounds present in the mushroom. MeThoD: Model optimization was carried out on PI3K, PTEN, mTOR, Akt, PDK1, FoxO1, GSK-3, MDM2, H-Ras, and BAD proteins in the PI3K/Akt/mTOR pathway and molecular docking of compounds/control inhibitors in the binding pocket were simulated AutoDock Vina in PyRx. The drug likeness, pharmacokinetic, and pharmacodynamic features of prospective docking leads were all anticipated. ReSulT: Several potent inhibitors of the selected key driver proteins in PI3K/Akt/mTOR pathway were identified from P ostreatus. Ellagic acid with binding affinities of −8.0, −8.0, −8.1, −8.2, −6.2, and −7.1 kcal/mol on PI3K, Akt, PDK1, GSK-3, MDM2, and BAD, respectively, had better binding affinity compared with their reference drugs. Likewise, apigenin (−7.8 kcal/mol), chrysin (−7.8 kcal/mol), quercetin (−6.4 kcal/ mol), and chlorogenic acid (−6.2 kcal/mol) had better binding affinities to PTEN, mTOR, FoxO1, and H-Ras proteins, respectively. ConCluSIon: Ellagic acid, apigenin, luteolin, quercetin, chlorogenic acid, chrysin, and naringenin phytochemicals are seen as the better lead molecules due to their ability to strongly bind to the proteins under study in this pathway. Analogs of these compounds can also be designed as potential drugs.
Targeting invasion-associated proteins PfSUB2 and PfTRAMP in Plasmodium falciparum: identification of potential inhibitors via molecular docking
(BMC Infectious Diseases, 2025) Okafor, Esther. O.; Bella-Omunagbe, Mercy; Elugbadebo, Temitope; Dokunmu, Titilope M.; Adebiyi, Ezekiel
Plasmodium falciparum subtilisin-like protease 2 (PfSUB2) is responsible for processing Plasmodium falciparum thrombospondin-related apical merozoite protein (PfTRAMP). These proteins are essential for asexual blood stage growth and RBC invasion and have, therefore, been identified as potential drug targets. This study predicted the three-dimensional structure of PfSUB2 and PfTRAMP and identified potential inhibitors using molecular docking methods. Five hundred nineteen compounds were docked against both proteins with AutoDock Vina in PyRx. Compounds 139,974,934 and 154,414,021 exhibited better binding affinities when compared to the standard inhibitors, PMSF, which highlights them as suitable inhibitors and potential antimalarials targeting PfTRAMP and PfSUB2. It also highlights 155,204,487 as a compound with dual antimalarial target potential, exhibiting a better binding affinity to PfTRAMP and PfSUB2. The study recommends 139,974,934, 154,414,021, and 155,204,487 as possible compounds for antimalarial drug development.