Protein glycosylation in Trypanosoma cruzi and mass spectrometry-based strategies for glycan and glycoprotein characterization
Rebeca Kawahara, Joyce Saad, Walter Colli, Maria JM Alves and Giuseppe Palmisano
from: Protozoan Parasitism: From Omics to Prevention and Control (Edited by: Luis Miguel de Pablos Torró and Jacob-Lorenzo Morales). Caister Academic Press, U.K. (2018) Pages: 49-64.
Trypanosoma cruzi is the protozoan parasite that causes Chagas disease. This parasite is genetically highly diverse and has a complex life cycle involving two different hosts and distinct developmental stages. The surface of the parasite is covered by a dense array of glycoproteins and glycolipids, which play important function in the differentiation processes and in the host-parasite interaction. The N- and O-glycan biosynthesis in T. cruzi has important features that involve unusual carbohydrates and glycosylation enzymes. The characterization of protein glycosylation in T. cruzi has unprecedented promise for the discovery of novel targets for drug design and therapeutic intervention in Chagas disease as well as to characterize the different T. cruzi strains. However, analytical methodologies for large-scale protein glycosylation analysis have faced challenges due to the extensive glycan micro- and macroheterogeneity. This chapter aims to provide an historical overview of key findings in T. cruzi protein glycosylation pathway, including the intermediates and enzymes involved especially in N-linked glycan biosynthesis and the analytical tools used to uncover the composition or structure of N and O-linked glycans. Moreover, we described how mass spectrometry is a powerful tool for large-scale characterizing the set of glycans and glycoproteins in T. cruzi read more ...