Comparative Proteomic Analysis of Lysine Acetylation in Trypanosomes

Comparative Proteomic Analysis of Lysine Acetylation in Trypanosomes

Author Moretti, Nilmar Silvio Autor UNIFESP Google Scholar
Cestari, Igor Google Scholar
Anupama, Atashi Google Scholar
Stuart, Ken Google Scholar
Schenkman, Sergio Autor UNIFESP Google Scholar
Abstract Protein acetylation is a post-translational modification regulating diverse cellular processes. By using proteomic approaches, we identified N-terminal and epsilon-lysine acetylated proteins in Trypanosoma cruzi and Trypanosoma brucei, which are protozoan parasites that cause significant human and animal diseases. We detected 288 lysine acetylation sites in 210 proteins of procyclic form, an insect stage of T. brucei, and 380 acetylation sites in 285 proteins in the form of the parasite that replicates in mammalian bloodstream. In T. cruzi insect proliferative form we found 389 epsilon-lysine-acetylated sites in 235 proteins. Notably, we found distinct acetylation profiles according to the developmental stage and species, with only 44 common proteins between T. brucei stages and 18 in common between the two species. While K-ac proteins from T. cruzi are enriched in enzymes involved in oxidation/reduction balance, required for the parasite survival in the host, in T. brucei, most K-ac proteins are enriched in metabolic processes, essential for its adaptation in its hosts. We also identified in both parasites a quite variable N-terminal acetylation sites. Our results suggest that protein acetylation is involved in differential regulation of multiple cellular processes in Trypanosomes, contributing to our understanding of the essential mechanisms for parasite infection and survival.
Keywords Trypanosoma brucei
Trypanosoma cruzi
mass spectrometry
xmlui.dri2xhtml.METS-1.0.item-coverage Washington
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo - FAPESP [2011/51973-3, 2015/22031-0, 2012/09403-8, 2013/20074-9]
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico - CNPq [477143/2011-3, 445655/2014-3]
Institute Nacional de Ciencia e Tecnologia de Vacinas from Brazil
National Institutes of Health [R01 AI078962]
American Heart Association fellowship [14POST18970046]
Grant number FAPESP [2011/51973-3, 2015/22031-0, 2012/09403-8, 2013/20074-9]
CNPq [477143/2011-3, 445655/2014-3]
Date 2018
Published in Journal Of Proteome Research. Washington, v. 17, n. 1, p. 374-385, 2018.
ISSN 1535-3893 (Sherpa/Romeo, impact factor)
Publisher Amer Chemical Soc
Extent 374-385
Access rights Closed access
Type Article
Web of Science ID WOS:000419749800035

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