Thank you.

Good afternoon everyone.

As that lovely introduction said, I'm Sophia Bird.

I'm from Lethbridge, Alberta, Canada.

And I just wanted to first off thank the sponsors and everyone who helped set up this convention.

And I'm very thankful to have the privilege of speaking to you all today and hearing about

everyone else's projects.

So once again, I will be discussing about multi-wavelength AUC.

I'll try and cut down on repeating a lot of the methods.

But again, I am going to be discussing one project that I worked on using multi-wavelength

analytical ultrasonarifugation to investigate a complexation between PLEASE-A, PLEASE-C,

which are these fill-Z domain proteins, and C. di-GMP.

So a brief quick overview of how the presentation will be laid out is I'll go into some introduction

information about the motivation of studying these proteins.

And then the previous interaction studies that have been published.

And then I'll go into my methods and results.

All right.

So these proteins and nucleotide that I had the privilege of working on are involved in

Lyme disease.

So Lyme disease is a bacterial infection that infects various mammalian hosts that is mainly

transmitted through ticks.

It was firstly diagnosed in Lyme, Connecticut, and has been a main health concern, most primarily

in the United States, with the CDC reporting 476,000 new cases every year.

So this disease can be treated with antibiotics within the first few days of the infection.

But 5% to 10% of patients still will experience chronic long-term effects, such as muscle

joint pain, as well as sleep and cognitive impairment.

So this study focuses on C. di-GMP, which is cyclic di-GMP, which is tied to the bacterial's

adaptation while they're in their larvae stage.

So when they come into contact with very nutritious blood, this nucleotide helps them regulate

their environment and basically not die.

So C. di-GMP binds to this PILZ domain that is present in two proteins that I was looking

into, PLEASE-A and PLEASE-C.

So this interaction isn't, its function isn't completely understood yet, but these studies

are looking into how there's this ligand-induced rearrangement.

So we're trying to first characterize the interaction in the complex to then see how

the bacteria use it in the tick and possibly in the mammalian hosts.

So previous interaction studies that have been published using ITC, x-ray diffraction,

and SAX data have shown that there's a one-to-one binding interaction with PLEASE-A, PLEASE-C,

and the C. di-GMP.

And in vivo studies have shown that in the absence of PLEASE-A in mammalian hosts, the

infection still occurs and can fester, basically, but the transmission between ticks in the

absence of PLEASE-A or a mutant PLEASE-A protein, the infection cannot be transmitted.

So there is a difference here.

So the study is trying to understand basically this interaction in ticks and understand the

environment in the infection between tick larvae.

And so the SAX data mainly highlighted this structural change upon binding.

So my methods and results involve multi-wavelength AUC.

To start off, I received all samples from our collaborators in Virginia and the University

of Montana.

And so I began taking the purified protein and nucleotide and did a dilution series and