Analyzing the Contribution of the Glutathione System Proteins in Oxidative Stress Resistance

Authors: Shivani Shah, Kara Swenson, James Konopka

SUNY Campus: Stony Brook University

Presentation Type: Poster

Location: Old Union Hall

Presentation #: 15

Timeslot: Session C 1:45-2:45 PM

Abstract: Candida albicans is a human fungal pathogen that around 50% of adults are colonized with. Neutrophils and macrophages in the innate immune system can uptake C. albicans through phagocytosis. The immune cell will then bombard C. albicans with toxic molecules such as superoxides. Those superoxides are produced by the phagosome membrane containing NADPH oxidase. Superoxides are very reactive which makes them efficient as tools of oxidative stress. When they react with proteins, lipids, or DNA, organic peroxides can form. C. albicans will then attempt to detoxify those organic peroxides and avoid further propagation of reactive oxygen species. Since the cell membrane is made of lipids, oxidative stress can produce a phenomenon called lipid peroxidation that can impact it. One major antioxidant system that is common across eukaryotes, including humans and C. albicans, is the glutathione system, which uses the small tripeptide, glutathione to protect against oxidative damage. Glutathione is used by antioxidant proteins to promote the reduction of oxidized molecules via sulfur residues on conserved cysteines.This project characterizes four genes from the glutathione system and their role as antioxidants. This characterization was done by utilizing green fluorescent protein tagging, CRISPR gene deletion, disk diffusion halo assays, and lipid peroxidation sensitivity spot assays.