Metabolic labeling of surface neo-sialylglyconjugates catalyzed by trypanosoma cruzi trans-sialidase

LANTOS, ANDRÉS B.; SOMOZA, MARTÍN; MUCCI, JUAN; CÁNEPA, GASPAR E.; BUSCAGLIA, CARLOS A.; CARLEVARO, GIANNINA; DE LOS MILAGROS CÁMARA, MARÍA; CAMPETELLA, OSCAR

METHODS IN MOLECULAR BIOLOGY (CLIFTON, N.J.)

Humana Press Inc.

Año: 2019 vol. 1955 p. 135 - 146

1064-3745

Trypanosoma cruzi, the protozoan agent of Chagas disease, has evolved an innovative metabolic pathway by which protective sialic acid (SA) residues are scavenged from host sialylglycoconjugates and transferred onto parasite surface mucin-like molecules (or surface glycoconjugates from host target cells) by means of a unique trans-sialidase (TS) enzyme. TS-induced changes in the glycoprotein sialylation profile of both parasite and host cells are crucial for the establishment of a persistent T. cruzi infection and for the development of Chagas disease-associated pathogenesis. In this chapter, we describe a novel metabolic labeling method developed in our labs that enables straightforward identification and molecular characterization of SA acceptors of the TS-catalyzed reaction.