The parasitic protist Trichomonas vaginalis is the causative agent of trichomoniasis, a highly prevalent sexually transmitted infection. The organism is known to accumulate substantial deposits of the polysaccharide glycogen, which is believed to serve as a store of carbon and energy that can be tapped during periods of nutrient limitation. Such nutrient limitation is likely to occur when T. vaginalis is transmitted between hosts, implying that glycogen may play an important role in the lifecycle of the parasite. Both T. vaginalis glycogen synthase and glycogen phosphorylase, key enzymes of glycogen synthesis and degradation, respectively, have been cloned and characterized, and neither enzyme is subject to the post-translational controls found in other, well-characterized eukaryotic systems. Thus, it is unclear how glycogen metabolism is regulated in this organism. Here we use a glucose limitation/re-feeding protocol to show that the activities of key enzymes of glycogen synthesis do not increase during re-feeding when glycogen synthesis is stimulated. Rather, a simple model appears to operate with glycogen storage being driven by the extracellular glucose concentration.

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