Functional analysis of S-31-D, a point mutant of Na-far-1 mimicking a phosphorilated state

JOSE F. LOMBARDO; GISELA R. FRANCHINI

Rosario

Congreso; L Reunión Anual de la Sociedad Argentina de Biofísica; 2022

Sociedad Argentina de Biofísica

Parasitic nematodes are a global problem and cause prolonged and potentially lethal infections. Human hookworms infect over 300 million people worldwide and are a significant problem in Argentina and South America. We are focused on the functional analysis of a group of proteins that are nematode specific and are conserved in both freeliving and parasitic species: the fatty acid and retinol binding proteins (FAR). These lipidbinding proteins are hypothesized to bind lipids required for nematode development and/or to manipulate host defense mechanisms, but their specific functions are still unknown.Given the biological importance of these proteins, our work focuses on Na-FAR-1, the FAR protein from Necator americanus, which has been successfully produced and characterized in our lab. These proteins have a conserved phosphorylation site that has not been studied yet and we hypothesize that it might alter its capability to bind different fatty acids and affect its stability, working as a possible regulatory site. To explore this possibility, we have obtained the Na-far-1 recombinant protein along with a genetically mutated protein with a single point mutation in the phosphorylation site, changing a Ser for an Aspartic acid, in order to simulate a phosphorylated state. We are currently carrying different fluorimetric experiments to compare these protein´s characteristics.