Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.
Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.
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全球对弓形虫弓形虫中棕榈酰化蛋白的分析。
DOI：
10.1016/j.chom.2015.09.006
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发表时间：
2015-10-14
影响因子：
30.3
通讯作者：
Bogyo M
中科院分区：
文献类型：
--
作者：
Foe IT;Child MA;Majmudar JD;Krishnamurthy S;van der Linden WA;Ward GE;Martin BR;Bogyo M
翻译后修饰（PTMs）如棕榈酰化是关键的原生动物寄生虫弓形虫的裂解周期。虽然棕榈酰化参与了入侵、运动和细胞形态，但利用这种PTM的蛋白质在很大程度上仍然未知。利用化学蛋白质组学方法，我们报告了对弓形虫棕榈酰化蛋白的综合分析，鉴定出总共282种蛋白，包括胞质蛋白、膜相关蛋白和跨膜蛋白。从这个大的棕榈酰化靶标集，我们验证了棕榈酰化蛋白参与运动（肌球蛋白轻链1，肌球蛋白A），细胞形态（PhIL1）和宿主细胞侵袭（顶膜抗原1，AMA1）。进一步研究表明，阻断棕榈酰化可增强顶端分泌细胞器中AMA1和其他侵袭相关蛋白的释放，表明AMA1控制着这一分泌过程。这些发现表明棕榈酰化在弓形虫蛋白质组中普遍存在，并揭示了这种重要人类病原体的生物学特性。
Post-translational modifications (PTMs) such as palmitoylation are critical for the lytic cycle of the protozoan parasite Toxoplasma gondii. While palmitoylation is involved in invasion, motility, and cell morphology, the proteins that utilize this PTM remain largely unknown. Using a chemical proteomic approach, we report a comprehensive analysis of palmitoylated proteins in T. gondii, identifying a total of 282 proteins, including cytosolic, membrane-associated and transmembrane proteins. From this large set of palmitoylated targets, we validate palmitoylation of proteins involved in motility (myosin light chain 1, myosin A), cell morphology (PhIL1), and host-cell invasion (apical membrane antigen 1, AMA1). Further studies reveal that blocking palmitoylation enhances the release of AMA1 and other invasion-related proteins from apical secretory organelles, suggesting that AMA1 controls this secretion process. These findings suggest that palmitoylation is ubiquitous throughout the T. gondii proteome and reveal insights into the biology of this important human pathogen.