Protein palmitoylation inhibition by 2-bromopalmitate alters gliding, host cell invasion and parasite morphology in Toxoplasma gondii
Protein palmitoylation inhibition by 2-bromopalmitate alters gliding, host cell invasion and parasite morphology in Toxoplasma gondii
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DOI：
10.1016/j.molbiopara.2012.03.006
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发表时间：
2012-07-01
影响因子：
1.5
通讯作者：
Corvi, M. M.
中科院分区：
文献类型：
--
作者：
Alonso, A. M.;Coceres, V. M.;Corvi, M. M.
蛋白质棕榈酰化是棕榈酸与蛋白质的可逆共价连接。这种翻译后修饰已被证明在信号转导、细胞定位和蛋白质活性调节等多种过程中发挥作用。尽管蛋白质棕榈酰化的许多方面已在哺乳动物和酵母细胞中得到鉴定，但人们对弓形虫中的这种修饰知之甚少。为了确定弓形虫中蛋白质棕榈酰化的功能作用，用棕榈酰化抑制剂 2-溴棕榈酸酯 (2-BP) 处理速殖子。用 2-BP 处理的寄生虫显示出非圆形轨迹显着增加，这些轨迹比未经处理的寄生虫留下的轨迹更长。此外，2-BP处理减少了对宿主细胞的侵袭过程。细胞内速殖子的长期治疗导致寄生虫形态和形状以剂量依赖性方式发生重大变化。这些结果表明，棕榈酰化可能正在修饰弓形虫中在滑动、侵袭和细胞骨架蛋白中起关键作用的蛋白质。 (C) 2012 Elsevier B.V. 保留所有权利。
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. (C) 2012 Elsevier B.V. All rights reserved.