Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor

Abstract

Trypanosoma cruzi is the etiologic agent of Chagas disease, a parasitic disease of great medical importance on the American continent. Trypomastigote infection’s initial step in a mammalian host is vital for the parasite’s life cycle. A trypomastigote’s surface presents many molecules, some of which have been proposed to be involved in the infection process, including a glycoprotein family called mucin-associated surface proteins (MASPs). This work describes a 49-kDa molecule (MASP49) that belongs to this family and is expressed mainly on the surfaces of amastigotes and trypomastigotes but can be found in extracts and the membrane-enriched fractions of epimastigotes. This protein is partially GPI-anchored to the surface and has a role during the internalization process, since its blockade with specific antibodies decreases parasite entry into Vero cells by 62%. This work shows that MASP49 binds to peritoneal macrophages and rat cardiomyocytes, undergoes glycosylation via galactose N-acetylgalactosamine, and can attach to the macrophage murine C-type lectin receptor (mMGL). These results suggest that MASP49 can be considered a virulence factor in T. cruzi, and a better understanding of its role in the infection process is necessary.

The End Justifies the Means: Chagas Disease from a Perspective of the Host–Trypanosoma cruzi Interaction

“…MASPs are overexpressed in the infective stages of the parasite (metacyclic and bloodstream trypomastigotes), being involved in host cell invasion, as was described by De Pablos and collaborators [41] studying MASP52. Recently, MASP49 was shown to bind to the C-type lectin receptor (mMGL) of murine peritoneal macrophages [42], contributing to cell invasion. Also, MASPs overexpression on the amastigotes membrane before division suggests that these proteins can play a role in the survival and multiplication of the intracellular amastigotes [43].…”

Possible Chemotherapeutic Potential of Inhibiting N-Alpha Terminal Acetylation Activities to Combat Trypanosome Infections

“…The plethora of MASP and the second largest gene family in T. cruzi, have been presented [105], suggesting that MASP is involved in mechanisms of host-parasite interactions. Furthermore, it is necessary for the infection process, as shown by analyzing mucin-associated surface protein 49 (MASP49) [106].…”