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Description
The cystic fibrosis transmembrane conductance regulator (CFTR) protein functions as an ion channel that transports ions including chloride and bicarbonate across the apical membrane of epithelial cells. Mutations in CFTR result in abnormal ion transport, causing the disease Cystic Fibrosis (CF). CF pathology is defined by thick mucus buildup throughout the body, blocking passageways to regions including the lungs and digestive track. Thick mucus buildup allows for the accumulation of bacterial biofilms. The symptoms of CF eventually result in an early death. While the function of the CFTR protein has been characterized in mammals, extensive investigations into the evolution of the CFTR protein is lacking. The focus of this work is to understand the evolutionary conservation of the CFTR protein in the organism Hydra vulgaris AEP strain. This may also provide a new model organism for future CF research as better model organisms to study this disease are needed. Hydra spp. belong to the phylum Cnidaria and are basal organisms to all metazoan life. They are complex organisms, however, and have conserved immune system components and mucous-secreting cells. Through bioinformatic analyses described here, a CFTR-like protein was identified in Hydra magnipapillata (a close genetic relative of H. vulgaris (AEP)) that contains necessary domains for conserved CFTR function. Pharmacological inhibitors were used to test the function of the CFTR protein in H. vulgaris (AEP). H. vulgaris (AEP) treated with specific CFTR inhibitors exhibited increased mortality, morbidity and susceptibility to bacterial infection compared to controls. H. vulgaris (AEP) exposed to CFTR inhibitor and CF therapies exhibited lower morbidity rates, suggesting functional conservation of the CFTR-like protein. Taken together, these data suggest H. vulgaris (AEP) may provide a novel model organism for future CF research.
