Metabolic Labeling of Surface Neo-sialylglyconjugates Catalyzed by Trypanosoma cruzi trans-Sialidase.
Carlevaro, G., Lantos, A. B., Canepa, G. E., de Los Milagros Camara, M., Somoza, M., Buscaglia, C. A., Campetella, O. and Mucci, J.
Instituto de Investigaciones Biotecnologicas, Universidad Nacional de San Martin, San Martin, Buenos Aires, Argentina.
Consejo Nacional de Investigaciones Cientificas y Tecnicas, Buenos Aires, Argentina.
Laboratorio Dr. Lantos, Buenos Aires, Argentina.
Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD, USA.
Instituto de Tecnologia, Universidad Argentina de la Empresa (UADE), Buenos Aires, Argentina.
Instituto de Investigaciones Biotecnologicas, Universidad Nacional de San Martin, San Martin, Buenos Aires, Argentina. jmucci@unsam.edu.ar.
Consejo Nacional de Investigaciones Cientificas y Tecnicas, Buenos Aires, Argentina. jmucci@unsam.edu.ar.
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.
Methods in Molecular Biology 1955: 135-146 (2019)