info:eu-repo/semantics/article
Protein palmitoylation inhibition by 2-bromopalmitate alters gliding, host cell invasion and parasite morphology in Toxoplasma gondii
Fecha
2012-07Registro en:
Alonso, Andrés Mariano; Cóceres, Verónica Mabel; de Napoli, Maximiliano Gabriel; Nieto Guil, Alvaro Fernando; Ángel, Sergio Oscar; et al.; Protein palmitoylation inhibition by 2-bromopalmitate alters gliding, host cell invasion and parasite morphology in Toxoplasma gondii; Elsevier Science; Molecular and Biochemical Parasitology; 184; 1; 7-2012; 39-43
0166-6851
CONICET Digital
CONICET
Autor
Alonso, Andrés Mariano
Cóceres, Verónica Mabel
de Napoli, Maximiliano Gabriel
Nieto Guil, Alvaro Fernando
Ángel, Sergio Oscar
Corvi, Maria Martha
Resumen
Protein palmitoylation is the reversible covalent attachment of palmitic acid onto proteins. This post-translational modification has been shown to play a part in diverse processes such as signal transduction, cellular localization and regulation of protein activity. Although many aspects of protein palmitoylation have been identified in mammalian and yeast cells, little is known of this modification in Toxoplasma gondii. In order to determine the functional role of protein palmitoylation in T. gondii, tachyzoites were treated with the palmitoylation inhibitor 2-bromopalmitate (2-BP). Parasites treated with 2-BP displayed a significant increase in non-circular trails which were longer than those trails left by non-treated parasites. Furthermore, 2-BP treatment reduced the invasion process to the host cells. Long-term treatment of intracellular tachyzoites resulted in major changes in parasite morphology and shape in a dose-dependent manner. These results suggest that palmitoylation could be modifying proteins that are key players in gliding, invasion and cytoskeletal proteins in T. gondii.