A novel Trypanosoma cruzi cAMP effector

Abstract

Although cAMP plays an essential role in Trypanosoma cruzi life cycle, the exact mechanisms of action are unknown. Up to date, Protein Kinase A (PKA) is the only known T. cruzi cAMP effector, however experimental evidences suggest the existence of other effectors. In order to identify new cAMP effectors, we carried out in silico studies using the predicted T. cruzi proteome. As a result, we identified 27 proteins with putative cAMP binding domains. Within these proteins, we subcloned and characterized the paralogs proteins TcCLB.508523.80 and TcCLB.507035.110, the two most solid candidates. Computational models shown that the domain present in these proteins could fold in a similar manner than other know cAMP effectors. In fact, both proteins could specifically bind cAMP. Moreover, transgenic T. cruzi epimastigotes expressing TcCLB.508523.80 shown an increased infectivity when incubated with 8-Br-cAMP. Our results indicate that TcCLB.508523.80 and TcCLB.507035.110 are bona fide cAMP binding proteins that could act as novel T. cruzi cAMP effectors during host cell infection.