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Novel mass spectrometry-based technologies for post-translational modifications analysis

Grant number: 21/14751-4
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): January 01, 2022
Effective date (End): December 31, 2023
Field of knowledge:Biological Sciences - Parasitology - Protozoology of Parasites
Principal researcher:Giuseppe Palmisano
Grantee:Simon Ngao Mule
Home Institution: Instituto de Ciências Biomédicas (ICB). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated research grant:18/15549-1 - Post-translational modifications in Chagas Disease biological processes and diagnostics: novel methodological approaches and biological applications, AP.JP2


Protein O-linked glycosylation is a post-translational modification (PTM) of proteins at serine or threonine hydroxyl functional groups. This PTM plays important roles including mammalian cell adhesion, functional determinants for antibody recognition, regulation of protein stability and activity, targeting of glycoproteins, and in host-parasite interaction where, for example, Trypanosoma cruzi, the etiological agent of Chagas disease (American Trypanosomiasis) interacts with host cells during recognition, adhesion and infection. This disease is a neglected tropical disease endemic in latin American countries, and that leads to cardiomyopathy, megaviscera or neurological complications in the chronic phase of the disease. A better understanding of T. cruzi-host interaction will help prioritize new therapeutic targets. Despite the key roles of protein O-linked glycosylation, method development strategies for this PTM has lagged behind. In the proposed study, the development of an analytical method for the study of O-linked glycoprotein will be sought. The development of new analytical methods for analyzing PTMs will offer the possibility to detect protein modifications in complex biological systems with high precision and sensitivity, expanding our current knowledge. In particular, the identification of protein glycosylation at different life stages of T. cruzi belonging to different genetic subdivisions (TcII and TcVI) and host cells will be evaluated and associated with the expression of specific glycosyltransferases. Large scale cell surface glycoproteome and glycome analysis combined with functional assays will be used as a molecular determinant linking glycosylation enzyme expression and phenotype. Inhibitors of protein glycosylation will be evaluated as potential chemotherapeutic target of T. cruzi.

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