Structural and functional characterization of a mannose binding protein (SM60) in Schistosoma mansoni

Abstract

For decades, studies that evaluate the complexity and immunogenicity of the tegument of Schistosoma mansoni has been conducted. This is because the membrane antigens associated with the surface on the tegument of S. mansoni have a great potential in vaccine development because they are exposed to the host immune system, but also are of great importance in biological studies of host-parasite interface. Among the discovered antigens, are Sm25, Sm16, Sm-TSP-1, Sm-TSP-2 and other proteins less characterized. In 2000, the SM60 was identified in our laboratory. This protein with lectin property (mannose linker) was described as an immunosuppressive molecule, reducing lymphoproliferation, and able to confer a significant protective effect in vivo (67%), which renders this lectin a potential target for the development of a vaccine against schistosomiasis. However, it is first necessary a more complete characterization, both structural and functional, this protein. And with this goal, this study aimed to isolate Sm60 of S. mansoni tegument, determine its amino acid sequence and identify the gene encoding this lectin. Later, we will assess the levels of Sm 60 gene expression in the evolutionary phases of S. mansoni, express it in a heterologous system to obtain this purified protein in greater amounts and conduct immunolocalization studies on evolutionary stages of the parasite. Thus, their role in host-parasite relationship may be evaluated. (AU)