A small proportion of the available HIF1A was hydroxylated and the levels of both PHD1 and PHD2 increased. Despite binding to EBNA-3, HIF1A was able to transactivate its target genes, including those involved in the glycolytic pathway. PDK1 phosphorylates the mitochondrial pyruvate dehydrogenase complex responsible for oxidative decarboxylation of pyruvate. The higher level of PDK1 suggests that the oxidative decarboxylation of pyruvate may be slower in LCLs. The level of GLUT1, a glucose transporter responsible for glucose uptake, is high in thyroid and colorectal cancers. PGK1, a phosphoglycerate kinase, is secreted by fibrosarcoma cells at levels several-fold higher than for normal fibroblasts. PKLR catalyzes the conversion of phosphoenolpyruvate and ADP into pyruvate and ATP in the last step of glycolysis. Hexokinase phosphorylates glucose into glucose-6-phosphate, which is the first step of the glycolytic pathway. At high oxygen concentration, glucose is metabolized to CO2 and the cells produce ATP and precursors for amino acid synthesis, whereas only minimal amounts of lactate are generated from pyruvate. At low oxygen concentrations, the cells convert most of the pyruvate to lactate and much less ATP is generated, in a process referred to as anaerobic glycolysis. However, the rate of ATP production is higher and overall metabolism is more efficient during glycolysis. Schistosomiasis is an important helminth infection and mainly occurs in developing countries. Despite decades of control, there are still millions of people at risk of contracting this infection. Current schistosomiasis Life Science Reagents control strategies are mainly based on safe and effective drugs, such as praziquantel and oxamniquine, but these do not prevent reinfection and the number of infected people has remained constant. The best long-term strategy to control schistosomiasis is through immunization with an antischistosomiasis vaccine combined with drug treatment. A vaccine that induces even a partial reduction in worm burdens could considerably reduce pathology and limit parasitic transmission. Recently, novel potential vaccine antigens were evaluated, but the level of protection obtained by vaccination with these antigens rarely exceeded the 40% benchmark set by the The World Health Organization. Therefore, it is necessary to search for alternative highly protective vaccine candidates. In all organisms, galactose metabolism is catalyzed by three enzymes: galactokinase, galactose-1-phosphate uridyltransferase, and uridine diphosphate galactose 49-epimerase. GALE catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose metabolism and it tightly binds the co-factor nicotinamide adenine dinucleotide required for catalytic activity. GALE also plays a pivotal role in the formation of extracellular polymeric substance, lipopolysaccharide, and capsular polysaccharide, which are related to biofilm formation. In humans, GALE deficiency results in an inborn error of metabolism, galactosemia. GALE also play an important role in the development of Drosophila melanogaster and Trypanosoma brucei. The gene encoding GALE also exists in Schistosoma japonicum; however, its specific function has not been elucidated. In the present study, we cloned and expressed full-length SjGALE cDNA and analyzed its expression level at different stages of schistosomal developmental and the localization of the protein. We also evaluated this protein as a vaccine candidate in vivo by examining the SjGALE-induced humoral and cellular immune protective mechanisms in a mouse model of schistosomal infection. An effective control strategy is to develop vaccines to prevent this disease.