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首页> 外文期刊>BMC Microbiology >Neisseria gonorrhoeae PIII has a role on NG1873 outer membrane localization and is involved in bacterial adhesion to human cervical and urethral epithelial cells
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Neisseria gonorrhoeae PIII has a role on NG1873 outer membrane localization and is involved in bacterial adhesion to human cervical and urethral epithelial cells

机译：淋病奈瑟氏球菌PIII在NG1873外膜定位中起作用，并参与细菌与人宫颈和尿道上皮细胞的粘附

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Background Protein PIII is one of the major outer membrane proteins of Neisseria gonorrhoeae, 95% identical to RmpM (reduction modifiable protein M) or class 4 protein of Neisseria meningitidis. RmpM is known to be a membrane protein associated by non-covalent bonds to the peptidoglycan layer and interacting with PorA/PorB porin complexes resulting in the stabilization of the bacterial membrane. The C-terminal domain of PIII (and RmpM) is highly homologous to members of the OmpA family, known to have a role in adhesion/invasion in many bacterial species. The contribution of PIII in the membrane architecture and its role in the interaction with epithelial cells has never been investigated. Results We generated a ΔpIII knock-out mutant strain and evaluated the effects of the loss of PIII expression on bacterial morphology and on outer membrane composition. Deletion of the pIII gene does not cause any alteration in bacterial morphology or sensitivity to detergents. Moreover, the expression profile of the main membrane proteins remains the same for the wild-type and knock-out strains, with the exception of the NG1873 which is not exported to the outer membrane and accumulates in the inner membrane in the ΔpIII knock-out mutant strain. We also show that purified PIII protein is able to bind human cervical and urethral cells and that the ΔpIII knock-out mutant strain has a lower ability to adhere to human cervical and urethral cells. Conclusion Here we demonstrated that the PIII protein does not play a key structural role in the membrane organization of gonococcus and does not induce major effects on the expression of the main outer membrane proteins. However, in the PIII knock-out strain, the NG1873 protein is not localized in the outer membrane as it is in the wild-type strain suggesting a possible interaction of PIII with NG1873. The evidence that PIII binds to human epithelial cells derived from the female and male genital tract highlights a possible role of PIII in the virulence of gonococcus and suggests that the structural homology to OmpA is conserved also at functional level.
机译：背景蛋白PIII是淋病奈瑟氏球菌的主要外膜蛋白之一，与脑膜炎奈瑟氏球菌的RmpM（可还原修饰的蛋白M）或4类蛋白有95％的同一性。已知RmpM是通过非共价键与肽聚糖层结合并与PorA / PorB孔蛋白复合物相互作用而导致细菌膜稳定的膜蛋白。 PIII（和RmpM）的C末端结构域与OmpA家族的成员高度同源，已知在许多细菌物种中，OmpA家族在粘附/侵袭中都有作用。从未研究过PIII在膜结构中的作用及其在与上皮细胞相互作用中的作用。结果我们产生了ΔpIII敲除突变体菌株，并评估了PIII表达损失对细菌形态和外膜组成的影响。 pIII基因的删除不会引起细菌形态或去污剂敏感性的任何改变。此外，对于野生型和敲除菌株，主要膜蛋白的表达谱保持相同，除了NG1873不会输出到外膜，而是在ΔpIII敲除中积聚在内膜中。突变株。我们还显示，纯化的PIII蛋白能够结合人宫颈和尿道细胞，而ΔpIII敲除突变株具有较低的粘附于人宫颈和尿道细胞的能力。结论在此我们证明，PIII蛋白在淋球菌的膜组织中不发挥关键的结构作用，并且不会对主要外膜蛋白的表达产生重大影响。但是，在PIII敲除菌株中，NG1873蛋白并不像在野生型菌株中那样位于外膜中，这表明PIII与NG1873可能存在相互作用。 PIII与源自雌性和雄性生殖道的人上皮细胞结合的证据突显了PIII在淋球菌毒性中的可能作用，并表明与OmpA的结构同源性在功能水平上也得以保守。

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