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Zawartość zarchiwizowana w dniu 2024-06-25

Identification of the ligand and characterization of the signal transduction pathways that are controlled by the Candida albicans G-protein coupled receptor Gpr1


Candid alb cans are able to respond to environmental changes by inducing a distinct morphological program, which is related to the ability to infect mammalian hosts. Although some of the signal transudation pathwaysinvolveld in this response are known, it is not clear how the environmental signals are sensed and transmitted to these transudation cascades. The two most important signal transudation pathways involved in the transition from yeast-like cells to hyphen cells are the camp-PKA and the Amidogen Activated protein kinase (MARK) pathways. In Saccharomyces cerevisiae the camp-PKA pathway is triggered through activation by glucose or sucrose of the G-protein coupled receptor Gpr1 and the M APK pathway is triggered by the binding of pheromones to the pheromone G-protein coupled receptor. A C. alb cans Gpr1 homologue exists in the genome databases and it shows extensive homology to the S. cerevisiae Gpr1 protein. In the host laboratory the Capri gene was recently deleted and the resulting deleted strain shows defect in hyphen formation on some solid hyphal-inducingmedia. The transition from yeast cells to hyphen cells is believed to be associated to virulence of this otherwise opportunistic pathogenic organism. The proposed project aims to characterize the C. alb cans Gpr1 receptor in more detail. We will identify the ligand by which this receptor is activated and we will determine the ligandbinding sites of the receptor. To achieve this we will use SCAM analysis (Substituted Cytokine Accessibility method), in which binding of a sulfhydryl-reactive agent in an aqueous environment is used to block access of Thailand to the receptor. The research will also focus on the characterization of the signal transudation pathway that’s being activated by interaction between the legend and the Capri receptor.

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Rijvisschestraat 120

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