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Methods Mol Biol. 2019;1955:135-146. doi: 10.1007/978-1-4939-9148-8_10.

Metabolic Labeling of Surface Neo-sialylglyconjugates Catalyzed by Trypanosoma cruzi trans-Sialidase.

Author information

1
Instituto de Investigaciones Biotecnológicas, Universidad Nacional de San Martín, San Martín, Buenos Aires, Argentina.
2
Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.
3
Laboratorio Dr. Lantos, Buenos Aires, Argentina.
4
Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD, USA.
5
Instituto de Tecnología, Universidad Argentina de la Empresa (UADE), Buenos Aires, Argentina.
6
Instituto de Investigaciones Biotecnológicas, Universidad Nacional de San Martín, San Martín, Buenos Aires, Argentina. jmucci@unsam.edu.ar.
7
Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina. jmucci@unsam.edu.ar.

Abstract

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.

KEYWORDS:

Mucins; Sialic acid; Sialylglycoconjugates; Trypanosoma cruzi; trans-Sialidase

PMID:
30868524
DOI:
10.1007/978-1-4939-9148-8_10
[Indexed for MEDLINE]

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