Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides.
Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides.
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DOI：
10.1038/ncomms3973
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发表时间：
2013
影响因子：
16.6
通讯作者：
Orth K
中科院分区：
文献类型：
--
作者：
Salomon D;Guo Y;Kinch LN;Grishin NV;Gardner KH;Orth K
细菌III型分泌系统将效应物递送到宿主细胞中以操纵细胞过程以利于病原体。这些效应物的许多宿主靶点在膜上发现。因此，为了鉴定它们的靶点，效应物通常使用专门的膜定位结构域来定位到适当的宿主膜。然而，许多领域使用的分子机制是未知的。在这里，我们确定了一个保守的细菌磷酸肌醇结合域（BPD），发现在功能多样的III型效应的植物和动物病原体。我们表明，BPD家族的成员在功能上结合磷酸肌醇和调解本地化的主机膜。此外，NMR研究表明，新鉴定的副溶血性弧菌III型效应子VopR的BPD在溶液中未折叠，但在结合其配体磷脂酰肌醇-（4，5）-二磷酸后折叠成特定结构。因此，我们的研究结果表明，一种可能的机制，促进再折叠的III型效应后，交付到宿主细胞。
Bacterial Type III Secretion Systems deliver effectors into host cells to manipulate cellular processes to the advantage of the pathogen. Many host targets of these effectors are found on membranes. Therefore, to identify their targets, effectors often use specialized membrane-localization domains to localize to appropriate host membranes. However, the molecular mechanisms used by many domains are unknown. Here we identify a conserved bacterial phosphoinositide-binding domain (BPD) that is found in functionally diverse Type III effectors of both plant and animal pathogens. We show that members of the BPD family functionally bind phosphoinositides and mediate localization to host membranes. Moreover, NMR studies reveal that the BPD of the newly identified Vibrio parahaemolyticus Type III effector VopR is unfolded in solution, but folds into a specific structure upon binding its ligand phosphatidylinositol-(4,5)-bisphosphate. Thus, our findings suggest a possible mechanism for promoting refolding of Type III effectors after delivery into host cells.