Identification of Trypanosoma cruzi proteins modified by S-nitrosylation and nitration after adhesion to extracellular matrix.

• Grant number: 12/03887-3
• Support Opportunities: Scholarships in Brazil - Master
• Start date: June 01, 2012
• End date: February 28, 2014
• Field of knowledge: Biological Sciences - Biochemistry - Biochemistry of Microorganisms
• Principal Investigator: Maria Julia Manso Alves
• Grantee: Milton César de Almeida Pereira
• Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil

Abstract

NO is a chemical messenger enzymatic synthesized from L-Arginine in many cell types and many organisms. Its actions involves, mainly, three different pathways: interaction with protein's metallic centers controlling its activity, activation of the enzyme guanylate cyclase fallowed by cGMP production, and covalent polypeptides modifications by S-nitrosylation at cysteine or nitration at tyrosine. Such covalent modifications are of great interest, due to its relationship with different physiological and phatophysiological processes, in many animals and plants. Even though this is a controversial subject in the specialized literature, the proteins modifications above-mentioned are being associated with intracellular signalization.The extracellular matrix (ECM) in the tissue participates in many physiological processes, such as intercellular communication. Trypanosoma cruzi interacts with ECM components, triggering responses both at the host cell (modulation of gene expression, for instance), and at the parasite itself. Despite its importance, the knowledge about the responses triggered at the parasite by the interaction with the ECM is only on the beginning. Altough the existence of NO synthase and the production of cGMP are already know, protein modifications by S-nitrosylation and nitration were hardly addressed.Since preliminary data from our laboratory indicates the occurrence of modifications by S-nitrosylation and nitration at parasite proteins incubated with ECM, the present project proposes the identification by MS/MS of proteins altered by S-nitrosylation and nitration as consequence of the parasite adhesion to the extracellular matrix. NO synthase role in this process will be verified by the utilization of specific inhibitors and NO quantification after the interaction between parasite and ECM.

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

MULE, S. N.; MANCHOLA, N. C.; DE OLIVEIRA, G. S.; PEREIRA, M.; MAGALHAES, R. D. M.; TEIXEIRA, A. A.; COLLI, W.; ALVES, M. J. M.; PALMISANO, G.. Proteome-wide modulation of S-nitrosylation in Trypanosoma cruzi trypomastigotes upon interaction with the host extracellular matrix. JOURNAL OF PROTEOMICS, v. 231, JAN 16 2021. (14/25494-9, 14/10046-0, 18/03727-2, 17/04032-5, 18/18257-1, 18/13283-4, 18/15549-1, 12/03887-3)

PEREIRA, MILTON; SOARES, CHRISLAINE; BAPTISTA CANUTO, GISELE ANDRE; MAGGI TAVARES, MARINA FRANCO; COLLI, WALTER; ALVES, MARIA JULIA M.. Down Regulation of NO Signaling in Trypanosoma cruzi upon Parasite-Extracellular Matrix Interaction: Changes in Protein Modification by Nitrosylation and Nitration. PLoS Neglected Tropical Diseases, v. 9, n. 4, APR 2015. (12/03887-3, 12/05621-0)

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

PEREIRA, Milton César de Almeida. Identification of proteins modified by S-nitrosylation and tyrosine nitration after adhesion of Trypanosoma cruzi to the extracellular matrix. 2014. Master's Dissertation - Universidade de São Paulo (USP). Conjunto das Químicas (IQ e FCF) (CQ/DBDCQ) São Paulo.