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PAAR-repeat proteins sharpen and diversify the type VI secretion system spike

机译：PAAR重复蛋白使VI型分泌系统的尖峰尖锐化并多样化

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摘要

The bacterial type VI secretion system (T6SS) is a large multicom-ponent, dynamic macromolecular machine that has an important role in the ecology of many Gram-negative bacteria. T6SS is responsible for translocation of a wide range of toxic effector molecules, allowing predatory cells to kill both prokaryotic as well as eukaryotic prey cells~(1-5). The T6SS organelle is functionally analogous to contractile tails of bacteriophages and is thought to attack cells by initially penetrating them with a trimeric protein complex called the VgrG spike~(6,7). Neither the exact protein composition of the T6SS organelle nor the mechanisms of effector selection and delivery are known. Here we report that proteins from the PAAR (proline-alanine-alanine-arginine) repeat superfamily form a sharp conical extension on the VgrG spike, which is further involved in attaching effector domains to the spike. The crystal structures of two PAAR-repeat proteins bound to VgrG-like partners show that these proteins sharpen the tip of the T6SS spike complex. We demonstrate that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae and Acinetobacter baylyi. Our results indicate a new model of the T6SS organelle in which the VgrG-PAAR spike complex is decorated with multiple effectors that are delivered simultaneously into target cells in a single contraction-driven translocation event.
机译：细菌VI型分泌系统（T6SS）是一种大型的多组分动态大分子机器，在许多革兰氏阴性细菌的生态学中具有重要作用。 T6SS负责转运多种毒性效应分子，使掠食性细胞杀死原核和真核猎物细胞（1-5）。 T6SS细胞器在功能上类似于噬菌体的可收缩尾巴，并被认为是通过最初用称为VgrG的三聚体蛋白复合物穿透细胞攻击细胞的（6,7）。 T6SS细胞器的确切蛋白质组成或效应子选择和传递的机制均未知。在这里，我们报告说，来自PAAR（脯氨酸-丙氨酸-丙氨酸-精氨酸）的蛋白质重复超家族在VgrG尖峰上形成了尖锐的圆锥形延伸，这进一步涉及将效应子结构域连接到尖峰上。与VgrG样伴侣结合的两种PAAR重复蛋白的晶体结构表明，这些蛋白可增强T6SS尖峰复合物的尖端。我们证明PAAR蛋白对于霍乱弧菌和贝氏不动杆菌的T6SS介导的分泌和靶细胞杀伤至关重要。我们的结果表明T6SS细胞器的新模型，其中VgrG-PAAR穗复合体装饰有多个效应子，这些效应子在单个收缩驱动的移位事件中同时传递到靶细胞中。

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  • 来源
    《Nature》 |2013年第7462期|350-353|共4页
  • 作者

    Mikhail M. Shneider; Sergey A. Buth; Brian T. Ho; Marek Basler; John J. Mekalanos; Petr G. Leiman;

  • 作者单位

    Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland,Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Molecular Bioengineering, 16/10Miklukho-Maklaya Street, 117997 Moscow, Russia;

    Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland;

    Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA;

    Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA;

    Department of Microbiology and Immunobiology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA;

    Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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