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首页> 外文期刊>Infection and immunity >The Major Outer Membrane Protein of Chlamydia psittaci Functions as a Porin-Like Ion Channel
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The Major Outer Membrane Protein of Chlamydia psittaci Functions as a Porin-Like Ion Channel

机译：鹦鹉热衣原体的主要外膜蛋白起着类似孔蛋白的离子通道的作用

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摘要

The major outer membrane protein (MOMP) of Chlamydiaspecies shares several biochemical properties with classical porin proteins. Secondary structure analysis by circular dichroism now reveals that MOMP purified from Chlamydia psittaci has a predominantly β-sheet content (62%), which is also typical of bacterial porins. Can MOMP form functional ion channels? To directly test the “porin channel” hypothesis at the molecular level, the MOMP was reconstituted into planar lipid bilayers, where it gave rise to multibarreled channels, probably trimers, which were modified by an anti-MOMP monoclonal antibody. These observations are consistent with the well-characterized homo-oligomeric nature of MOMP previously revealed by biochemical analysis and with the triple-barreled behavior of other porins. MOMP channels were weakly anion selective (P Cl/P K ～ 2) and permeable to ATP. They may therefore be a route by whichChlamydia can take advantage of host nucleoside triphosphates and explain why some anti-MOMP antibodies neutralize infection. These findings have broad implications on the search for an effective chlamydial vaccine to control the significant human and animal diseases caused by these organisms.
机译：衣原体的主要外膜蛋白（MOMP）与经典孔蛋白具有相同的生化特性。现在通过圆二色性的二级结构分析表明，从鹦鹉热衣原体纯化的MOMP主要具有β-折叠含量（62％），这也是细菌孔蛋白的典型特征。 MOMP可以形成功能性离子通道吗？为了在分子水平上直接测试“孔道”假说，将MOMP重构为平面脂质双层，在其中形成多管通道，可能是三聚体，并通过抗MOMP单克隆抗体对其进行了修饰。这些观察结果与先前通过生化分析揭示的MOMP的充分表征的低聚性质以及其他孔蛋白的三管行为一致。 MOMP通道具有弱阴离子选择性（ P Cl / P K 〜2），并且可渗透ATP。因此，它们可能是<衣原体>利用宿主核苷三磷酸的途径，并解释了为什么某些抗MOMP抗体能中和感染。这些发现对寻找有效的衣原体疫苗以控制由这些生物体引起的重大人类和动物疾病具有广泛的意义。

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