<i>T</i><i>rypanosoma cruzi trans</i>-sialidase as a multifunctional enzyme in Chagas’ disease

Trypanosoma cruzi trans-sialidase (TS) was identified three decades ago. TS catalyses a trans-glycosylation reaction, transferring SA from sialylated donors to the terminal galactose mucin-glycoconjugates, or non-mucin galactyosyl-glycoconjugates. It is an external surface protein that is also released from the parasite, displaying several binding properties in addition to its enzymatic function. TS structure has been solved and its catalytic properties are well known, providing tools for development of new inhibitors, as potential chemotherapeutic agents against Chagas' disease. However, there are still several unsolved questions regarding TS role in the biology of T. cruzi and in the pathology of Chagas' disease. In this review, we will describe the multifunctional roles of TS regarding the development of Chagas' disease and propose that these multiple functions have to be considered in future investigations aiming to use TS as a drug target.