Presentation Type

Poster

Abstract

Borrelia burgdorferi, the bacterium that causes Lyme disease, is transmitted between vertebrate hosts by a tick vector in an enzootic cycle. While in a mammal, B. burgdorferi uses the sugar glucose from the blood of its host as a source of carbon for glycolysis, a metabolic pathway that converts the glucose into energy. While in the tick, however, there is a period of time when the blood meal is consumed and a different source of carbon needs to be utilized. A set of genes called the glp operon allows B. burgdorferi to use the sugar alcohol glycerol as a carbon source during this time of nutrient stress. The third gene in the operon, encoding glycerol-3-phosphate dehydrogenase, is the gateway between using glycerol as a carbon source for energy or shuttling it into a different metabolic pathway for membrane synthesis. Crystal structures of GlpD from Escherichia coli reveal two parts: a catalytic, membrane-associated domain and a small soluble “cap” domain. Preliminary data on the RNA landscape of the glp operon suggest that the cap domain in B. burgdorferi is produced independently and made as a separate protein from the entire GlpD. I hypothesized that the cap domain has a regulatory function. I have accomplished my goal of purifying the cap domain from B. burgdorferi GlpD to near homogeneity and now plan to assay its ability to bind to different molecules in order to assess its function in B. burgdorferi. Additionally, I will test the conditions under which the bacterium synthesizes this independent cap domain, and eventually I will attempt to crystallize the cap domain in order to determine its structure.

Category

Life Sciences

Available for download on Sunday, April 19, 2020

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Apr 28th, 11:00 AM Apr 28th, 12:00 PM

The role of the GlpD cap domain in Borrelia burgdorferi

UC South Ballroom

Borrelia burgdorferi, the bacterium that causes Lyme disease, is transmitted between vertebrate hosts by a tick vector in an enzootic cycle. While in a mammal, B. burgdorferi uses the sugar glucose from the blood of its host as a source of carbon for glycolysis, a metabolic pathway that converts the glucose into energy. While in the tick, however, there is a period of time when the blood meal is consumed and a different source of carbon needs to be utilized. A set of genes called the glp operon allows B. burgdorferi to use the sugar alcohol glycerol as a carbon source during this time of nutrient stress. The third gene in the operon, encoding glycerol-3-phosphate dehydrogenase, is the gateway between using glycerol as a carbon source for energy or shuttling it into a different metabolic pathway for membrane synthesis. Crystal structures of GlpD from Escherichia coli reveal two parts: a catalytic, membrane-associated domain and a small soluble “cap” domain. Preliminary data on the RNA landscape of the glp operon suggest that the cap domain in B. burgdorferi is produced independently and made as a separate protein from the entire GlpD. I hypothesized that the cap domain has a regulatory function. I have accomplished my goal of purifying the cap domain from B. burgdorferi GlpD to near homogeneity and now plan to assay its ability to bind to different molecules in order to assess its function in B. burgdorferi. Additionally, I will test the conditions under which the bacterium synthesizes this independent cap domain, and eventually I will attempt to crystallize the cap domain in order to determine its structure.