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The disaccharide trehalose has been found to play diverse roles, from energy source to stress protectant, and this sugar is found in organisms as diverse as bacteria, fungi, plants, and invertebrates but not in mammals. Recent studies in the pathobiology ofCryptococcus neoformans identified the presence of a functioning trehalose pathway during infection and suggested its importance forC. neoformans survival in the host. Therefore, inC. neoformans we created null mutants of the trehalose-6-phosphate (T6P) synthase (TPS1 ), trehalose-6-phophate phosphatase (TPS2 ), and neutral trehalase (NTH1 ) genes. We found that bothTPS1 andTPS2 are required for high-temperature (37°C) growth and glycolysis but that the block atTPS2 results in the apparent toxic accumulation of T6P, which makes this enzyme a fungicidal target. Sorbitol suppresses the growth defect in thetps1 andtps2 mutants at 37°C, which supports the hypothesis that these sugars (trehalose and sorbitol) act primarily as stress protectants for proteins and membranes during exposure to high temperatures inC. neoformans . The essential nature of this pathway for disease was confirmed when atps1 mutant strain was found to be avirulent in both rabbits and mice. Furthermore, in the system of the invertebrateC. elegans , in which high in vivo temperature is no longer an environmental factor, attenuation in virulence was still noted with thetps1 mutant, and this supports the hypothesis that the trehalose pathway inC. neoformans is involved in more host survival mechanisms than simply high-temperature stresses and glycolysis. These studies inC. neoformans and previous studies in other pathogenic fungi support the view of the trehalose pathway as a selective fungicidal target for use in antifungal development.

Characterization and Regulation of the Trehalose Synthesis Pathway and Its Importance in the Pathogenicity of Cryptococcus neoformans