Metabolic Labeling of Surface Neo-sialylglyconjugates Catalyzed by Trypanosoma cruzi trans-Sialidase
| Autor: | Carlos A. Buscaglia, Juan Mucci, Andrés B. Lantos, María de los Milagros Camara, Oscar Campetella, Gaspar E. Canepa, Martín Somoza, Giannina Carlevaro |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
Chagas disease
Glycoconjugate Trypanosoma cruzi Blotting Western Protozoan Proteins Fluorescent Antibody Technique Neuraminidase Article Host-Parasite Interactions 03 medical and health sciences chemistry.chemical_compound parasitic diseases medicine Parasite hosting Animals Humans Chagas Disease 030304 developmental biology Glycoproteins chemistry.chemical_classification 0303 health sciences biology Staining and Labeling 030302 biochemistry & molecular biology biology.organism_classification medicine.disease Flow Cytometry N-Acetylneuraminic Acid Sialic acid Metabolic pathway Enzyme chemistry Biochemistry Glycoprotein Metabolic Networks and Pathways |
| Zdroj: | Methods in Molecular Biology ISBN: 9781493991471 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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