مشروع البحث:
Structure-function studies of Borrelia metal transport A (BmtA) from Lyme disease-causing Borrelia burgdorferi

dc.contributor.advisorProf. Geoff Gobert
dc.contributor.advisorDr. Edel Hyland.
dc.date.accessioned2026-05-31T07:16:30Z
dc.date.available2026-05-31T07:16:30Z
dc.descriptionGiven the essential role of manganese metabolism, we consider BmtA as a potential drug target for treating Lyme Disease. This project aimed to gain new insights into identifying BmtA amino acid residues that form the Mn²⁺ binding site, to understand substrate recognition and binding. This thesis sought to characterize the structural and functional characteristics. of BmtA, focusing on its metal-binding capacity and oligomeric state to assess its potential as a therapeutic target. A structural model of BmtA was generated using AlphaFold2, and bacterial ZIP crystallography, along with comparisons to mammalian ZIP transporters, were employed to identify the metal-binding site.
dc.description.abstractLyme disease is caused by the spirochetal bacterium Borrelia burgdorferi and continues to be the most prevalent vector-borne illness in humans (Singh & Girschick, 2004a). Identifying new drug targets is crucial for overcoming the challenges posed by Lyme disease, including antibiotic resistance (Baker, 2020), persistent infections (Aucott, Rebman, et al., 2013a), and complex disease dynamics (Aucott, Crowder, et al., 2013). Manganese (Mn2+) is the structural core of various enzymes supporting important biological processes, including oxidative phosphorylation, glycosylation, and signal transduction (Troxell et al., 2013).
dc.identifier1172
dc.identifier.urihttps://dspace.academy.edu.ly/handle/123456789/2106
dc.subject(BmtA) from Lyme disease-causing Borrelia burgdorferi
dc.titleStructure-function studies of Borrelia metal transport A (BmtA) from Lyme disease-causing Borrelia burgdorferi
dspace.entity.typeProject
project.endDate2025
project.funder.nameكيمياء حيوية
project.investigatorرجاء مسعود علي الأعور
project.startDate2024
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