X-ray structures of <Emphasis Type=Italic>Na</Emphasis>-GST-1 and <Emphasis Type=Italic>Na</Emphasis>-GST-2 two glutathione s-transferase from the human hookworm <Emphasis Type=Italic>Necator americanus</Emphasis>期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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.

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