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X-ray structures of Na-GST-1 and Na-GST-2 two glutathione s-transferase from the human hookworm Necator americanus
Authors:Oluwatoyin A Asojo  Kohei Homma  Meghan Sedlacek  Michelle Ngamelue  Gaddam N Goud  Bin Zhan  Vehid Deumic  Oluyomi Asojo  Peter J Hotez
Affiliation:(1) Department of Pathology and Microbiology, College of Medicine Nebraska Medical Center, Omaha, NE 68198-6495, USA;(2) Department of Microbiology, Immunology, and Tropical Medicine, The George Washington University Medical Center, Washington, DC 20037, USA
Abstract:

Background  

Human hookworm infection is a major cause of anemia and malnutrition of adults and children in the developing world. As part of on-going efforts to control hookworm infection, The Human Hookworm Vaccine Initiative has identified candidate vaccine antigens from the infective L3 larval stages and adult stages of the parasite. Adult stage antigens include the cytosolic glutathione-S-transferases (GSTs). Nematode GSTs facilitate the inactivation and degradation of a variety of electrophilic substrates (drugs) via the nucleophilic addition of reduced glutathione. Parasite GSTs also play significant roles in multi-drug resistance and the modulation of host-immune defense mechanisms.
Keywords:
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