Graduation Year
2017
Graduation Month
May
Document Type
Professional Paper - Campus Access Only
Degree Name
Bachelor of Science
School or Department
Biological Sciences, Division of
Major
Biology – Cellular and Molecular Biology
Faculty Mentor Department
Biological Sciences, Division of
Faculty Mentor
Dr. Scott Samuels
Keywords
Borrelia, GlpD, purification
Subject Categories
Integrative Biology
Abstract
Borrelia burgdorferi, the etiologic agent of Lyme disease, is transmitted among reservoir vertebrates by Ixodes ticks in an enzootic cycle. Naïve tick larvae acquire B. burgdorferi by feeding on infected vertebrates. Then, the larvae absorb their blood meal and molt into nymphs. B. burgdorferi reside in the tick midgut and switch from utilizing the sugar glucose, its preferred energy source, to the sugar alcohol glycerol, which is found in the tick as an antifreeze. The enzyme glycerol-3-phosphate (G3P) dehydrogenase, encoded by the gene glpD, is predicted to convert glycerol to dihydroxyacetone phosphate (DHAP), which enters glycolysis, the central metabolic pathway for energy production. The B. burgdorferi GlpD has been predicted based on homology to GlpD from other bacteria, yet this has not been biochemically confirmed and the enzyme has yet to be functionally characterized. We hypothesize that GlpD from B. burgdorferi has the same structure and function as GlpD from the model bacterium Escherichia coli. I expressed and obtained recombinant B. burgdorferi GlpD from E. coli. I will perform further purification of the partially purified GlpD prior to biochemical assay to analyze its activity, the conversion of G3P to DHAP.
Honors College Research Project
1
Recommended Citation
Zhou, Zhibing, "Purification and Functional Analysis of Glycerol-3-Phosphate Dehydrogenase (GlpD) from Borrelia burgdorferi" (2017). Undergraduate Theses, Professional Papers, and Capstone Artifacts. 172.
https://scholarworks.umt.edu/utpp/172
© Copyright 2017 Zhibing Zhou