Molecular characterization and functional analysis of Schistosoma mekongi neuroglobin homolog.

Schistosomes are blood-dwelling parasites that are constantly exposed to high-level oxidative stress arising from parasite-intrinsic and host defense mechanisms. To survive in their hosts, schistosomes require an antioxidant system to minimize with oxidative stress. Several schistosome antioxidant enzymes have been identified and have been suggested to play indispensable antioxidant roles for the parasite. In addition to antioxidant enzymes, non-enzymatic antioxidants including small molecules, peptides, and proteins have been identified and characterized. Neuroglobin (Ngb), a nervous system-specific heme-binding protein, has been classified as a non-enzymatic antioxidant and is capable of scavenging a variety of free radical species. The antioxidant activity of Ngb has been well-studied in humans. Ngb is involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging in the central and peripheral nervous systems, but its functions in schistosome parasites have not yet been characterized. In this study, we aimed to characterize the molecular properties and functions of Schistosoma mekongi Ngb (SmeNgb) using bioinformatic, biochemical, and molecular biology approaches. The amino acid sequence of Ngb was highly conserved among schistosomes as well as closely related trematodes. SmeNgb was abundantly localized in the gastrodermis, vitelline, and ovary of adult female S. mekongi worms as well as in the tegument of adult male worms. Assessment of antioxidant activity demonstrated that recombinant SmeNgb had Fe chelating and hydrogen peroxide scavenging activities. Intriguingly, siRNA silencing of SmeNgb gene expression resulted in tegument pathology. Understanding the properties and functions of SmNgb will help in future development of effective treatments and vaccines against S. mekongi, other schistosome parasites, and other platyhelminths.