Trypanosoma cruzi trans-sialidase as a multifunctional enzyme in Chagas’ disease

Abstract

Summary 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.

Proteomic analysis reveals different composition of extracellular vesicles released by two Trypanosoma cruzi strains associated with their distinct interaction with host cells

“…In contrast, we detected the presence of the group II more abundantly in the Y-EVs, which correspond to the 85 kDa family of glycoproteins involved in the parasite interaction with host cells. Those proteins harbour the typical FLY sequence and two sialidase domains [4,5,23,42] and monoclonal antibodies against one set of these proteins, called Tc85, partially inhibits the host’s cell invasion by the parasite [43]. …”

Virulence factors of Trypanosoma cruzi: who is who?

“…In fact, several pieces of evidence suggest that T. cruzi TS is also involved in a wide range of mechanisms related to parasite virulence like complement resistance, immunosuppression, thrombocytopenia and apoptosis of mouse thymocytes [77,78].…”

Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi

“…Instead T. cruzi expresses a trans-sialidase (TS), which intriguingly transfers sialic acid from host glycoconjugates to the terminal galactosyl residues of mucin-or non-mucin glycoconjugates expressed by the parasite [12,[40][41][42].…”