Lyme disease, caused by the bacteria Borrelia burgdorferi, is the fastest growing and most common tick-borne illness in the United States. B. burgdorferi is transferred to humans via tick bites and infection can cause long term illnesses including chronic arthritis. To survive the numerous environments it encounters during its life cycle, B. burgdorferi has complex regulatory pathways to deal with the stress of changing temperatures, pH, oxidization environments, and blood compositions between hosts. The Borrelia oxidative stress regulator, BosR, is a regulatory transcription factor that is vital to the survival of B. burgdorferi in all of its hosts. It functions to activate and repress nearly 80 genes, including genes for DNA protection from damage during starvation or oxidative stress and control over the expression of outer membrane proteins which are important for colonization in mammals. The goal of this research is to rigorously characterize the metal binding properties of BosR and to determine the relationship between metal and DNA binding. Classification of the metal interactions, along with identification of a specific Bos box, will aid in discovering additional genes that may be under the control of BosR and provide further understanding into the workings of this disease. This work determines the role of the amino acid in the position 39 of the protein, a common mutation observed, in DNA binding. The differences between the wild type and mutant binding to regulatory sequences of DNA show that the amino acid at position 39 is very important for binding interactions.

What makes Lyme disease tick?  Impact on DNA-protein interactions by mutations to regulator BosR

249th National Meeting (2015)

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