Graduation Year

2018

Graduation Month

May

Document Type

Thesis - Campus Access Only

Degree Name

Bachelor of Science

School or Department

Biochemistry and Biophysics Program

Major

Biochemistry

Faculty Mentor

Scott Samuels

Faculty Mentor Department

Biological Sciences, Division of

Subject Categories

Biochemistry, Biophysics, and Structural Biology | Molecular Biology

Abstract

The bacterium Borrelia burgdorferi causes Lyme disease, the most common tick-borne illness in the Northern hemisphere. The bacterium lives in an enzootic cycle, transiting between a tick vector and a vertebrate host. While in the tick, B. burgdorferi uses glucose from the blood meal as a carbon source for glycolysis, a catabolic pathway that produces energy. When the blood meal is digested and absorbed by the tick midgut, the bacterium must find a different source of carbon to survive. Glycerol, a three-carbon sugar alcohol used as an anti-freeze in the tick, can serve as a substitute carbon source for glycolysis during this period of nutrient stress. A set of genes called the glp operon encode the molecular machinery to utilize glycerol. The last gene in the operon, glpD, encodes glycerol-3-phosphate dehydrogenase, which is the gateway that shuttles glycerol to either glycolysis (as an energy source) or membrane biosynthesis. The GlpD enzyme appears to have two domains: an FADH2-binding domain and a small “cap” domain. Preliminary data suggest that the cap domain may be made as an independent protein. The cap domain was overexpressed and purified to determine its functional role in B. burgdorferi. Further analyses will be done to determine structure and enzymatic activity.

Honors College Research Project

Yes

Available for download on Friday, February 14, 2025

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© Copyright 2018 Bethany Crouse