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article imageBody's own enzymes unleashed to combat parasites

By Tim Sandle     Oct 8, 2014 in Science
A common type of enzyme, found in the human body, has the potential to fight parasitic diseases like sleeping sickness. In a new study, scientists found that by blocking the activity of the enzyme kills a range of parasites.
The enzyme is called pyruvate kinase. The new research suggests that inhibiting this enzyme kills the parasite while not affecting the infected person. The finding came about after hundreds of laboratory studies were conducted to see how pyruvate kinase functions in parasites, mammals and bacteria. The research uncovered that the enzyme carries out the same function, but it becomes active in all species in very different ways. In terms of its function in cells, a small sugar molecule binds to the enzyme to initiate a process called nutrient absorption (or glycolysis).
What is of scientific interest is that each species has its own mechanism for activating the enzyme. This means that some species — like parasites — can be disrupted whereas other species can be left unaffected.
Although trials are ongoing, the researchers behind the study hope that work can begin on tackling the parasites that cause sleeping sickness and Chagas disease. Sleeping sickness is a parasitic disease of people and animals (usually carried by the tsetse fly in rural areas). The disease is is characterized by fever, headaches, joint pains, and itching. Fever is intermittent, with attacks lasting from a day to a week.
Chagas disease is a tropical parasitic disease. It is spread mostly by insects known as Triatominae or kissing bugs. The disease, in the chronic stage, affects the nervous system, digestive system and heart. About two-thirds of people with chronic symptoms have cardiac damage.
The discovery provides an opportunity to design drugs that block activity of the enzyme. The findings have been published in the journal Royal Society Open Science. The research is titled “Structures of pyruvate kinases display evolutionarily divergent allosteric strategies.”
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