Molecular characterization and functional analysis of Schistosoma mekongi neuroglobin homolog

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 Fe2+ 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.PMID:35364046 | DOI:10.1016/j.actatropica.2022.106433
Source: Acta Tropica - Category: Infectious Diseases Authors: Source Type: research