Protein palmitoylation inhibition by 2-bromopalmitate alters gliding, host cell invasion and parasite morphology in Toxoplasma gondii

ALONSO AM; COCERES VM; DE NAPOLI MG; NIETO GUIL AF; ANGEL SO; CORVI MM

MOLECULAR AND BIOCHEMICAL PARASITOLOGY

ELSEVIER SCIENCE BV

Año: 2012 p. 39 - 43

0166-6851

23 Protein palmitoylation is the reversible covalent attachment of palmitic acid24 onto proteins. This post-translational modification has been shown to play a part25 in diverse processes such as signal transduction, cellular localization and26 regulation of protein activity. Although many aspects of protein palmitoylation27 have been identified in mammalian and yeast cells, little is known of this28 modification in Toxoplasma gondii. In order to determine the functional role of29 protein palmitoylation in T. gondii, tachyzoites were treated with the30 palmitoylation inhibitor 2-bromopalmitate (2-BP). Parasites treated with 2-BP31 displayed a significant increase in non-circular trails which were longer than32 those trails left by non-treated parasites. Furthermore, 2-BP treatment reduced33 the invasion process to the host cells. Long-term treatment of intracellular34 tachyzoites resulted in major changes in parasite morphology and shape in a35 dose-dependent manner. These results suggest that palmitoylation could be36 modifying proteins that are key players in gliding, invasion and cytoskeletal37 proteins in T. gondii.