李斯特菌诱导宿主细胞骨架重排与磷脂酶D

无论是免疫细胞对病原体的主动吞噬,还是病原体诱导非吞噬细胞的被动吞噬,均是不同细胞膜受体介导的细胞肌动蛋白骨架重排过程,受到单体G蛋白和肌动蛋白骨架相关蛋白的精密调控。细胞内重要信号蛋白,磷脂酰胆碱专一性磷脂酶D(PLD)的活性变化与细胞肌动蛋白骨架重排密切相关,其参与调节了由抗体受体(FcγR)及补体受体(CR3)介导的免疫细胞的主动吞噬,而细胞肌动蛋白骨架解聚蛋白cofilin被磷酸化后可与PLD结合并激活PLD,进而调节肌动蛋白骨架重排。另一方面,cofilin磷酸化状态严格调控李斯特菌感染细胞过程中的肌动蛋白骨架重排。因此,阐明PLD是否在李斯特菌感染细胞过程中被激活并参与调节肌动蛋白骨架重排,将有助于揭示PLD激活对感染发生的调控作用,对透彻理解细菌感染宿主细胞的分子机制具有重要意义。

Listeria-induced host cellular actin cytoskeleton rearrangement and phospholipase D

Either phagocytosis of macrophage to pathogen or pathogen-induced invasion into non-professional phagocytes, such as epithelial cells, require actin cytoskeletal rearrangements and remodeling of the plasma membrane, which are regulated precisely by monogeric GTPase and the correlated proteins. As a key signaling molecule in the cell, phosphotidicphospholipase D (PLD) regulates or interacts directly with cellular actin cytoskeleton rearrangement. Phospholipase D plays an important role in FcgammaRI and C-reactive protein-mediated phagocytosis and phosphorylated cofilin, a ADF (actin depolymerizing factor) is able to bind to phospholipase D and stimulate it; meanwhile, the Listeria-induced actin cytoskeleton rearrangement during the infection is controlled by the phosphorylation of cofilin. Thus, it made challenge to disclose the function of PLD on the regulation of Listeria-induced actin cytoskeleton rearrangement during infection, furthermore, it may provide us more understanding on the role of PLD in the infection and inflammation, which is essential to dissect the molecular mechanism of bacterial-host interaction more thoroughly.