Septin associating proteins in Candida albicans

Advisor Information

Jill Blankenship

Location

Dr. C.C. and Mabel L. Criss Library

Presentation Type

Poster

Start Date

7-3-2014 9:00 AM

End Date

7-3-2014 12:00 PM

Abstract

Candida albicans is a significant human pathogen as well as part of the natural microbial flora of most humans. Our interests center on the pathogenesis and antifungal drug susceptibility of this organism, and we focus on a family of proteins, the septins, that are involved in this process. Septins play a key role in filamentation, are vital to pathogenesis, and are important to cell wall integrity. Other roles involve cell cycle progression and acting as a protein scaffold at septation sites. This scaffold allows for the binding and recruitment of proteins. The ultimate goal of this project is to identify proteins associated with septins in C. albicans. I have designed and built a construct that adds a His6 tag to the essential septin CDC3, which is being used in pull-down assays to isolate the native septin complex and associated proteins. I will discuss the construction of this tagged strain and my efforts to develop methods to isolate the septin complex from C. albicans. This work has the potential to uncover novel septin interactions with regulatory and signaling elements which will advance our understanding of C. albicans as a pathogen.

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COinS
 
Mar 7th, 9:00 AM Mar 7th, 12:00 PM

Septin associating proteins in Candida albicans

Dr. C.C. and Mabel L. Criss Library

Candida albicans is a significant human pathogen as well as part of the natural microbial flora of most humans. Our interests center on the pathogenesis and antifungal drug susceptibility of this organism, and we focus on a family of proteins, the septins, that are involved in this process. Septins play a key role in filamentation, are vital to pathogenesis, and are important to cell wall integrity. Other roles involve cell cycle progression and acting as a protein scaffold at septation sites. This scaffold allows for the binding and recruitment of proteins. The ultimate goal of this project is to identify proteins associated with septins in C. albicans. I have designed and built a construct that adds a His6 tag to the essential septin CDC3, which is being used in pull-down assays to isolate the native septin complex and associated proteins. I will discuss the construction of this tagged strain and my efforts to develop methods to isolate the septin complex from C. albicans. This work has the potential to uncover novel septin interactions with regulatory and signaling elements which will advance our understanding of C. albicans as a pathogen.