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

ALONSO AM; COCERES V; DE NAPOLI M G; NIETO GUIL A; ANGEL SO; CORVI MM

MOLECULAR AND BIOCHEMICAL PARASITOLOGY

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2012

0166-6851

Protein palmitoylation refers to 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 widely used inhibitor 2-bromopalmitate (2-BP) and different biologically processes were tested. Incubation of parasites with 2-BP displayed a significant increase in non-circular trails and these trails were significantly longer than those trails left by non-treated parasites. Furthermore, 2-BP treatment reduced the invasion process to the host cells. Long treatment of intracellular tachyzoites showed serious changes in parasite morphology and shape. These results suggest that palmitoylation could be modifying proteins that are key players in gliding, invasion and cytoskeletal proteins in T. gondii.