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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi
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Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi

机译：晶体结构的n端结构域主要毒性因素BB0323莱姆包柔氏螺旋体病代理burgdorferi

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摘要

Lyme disease is an infection caused by the spirochete Borrelia burgdorferi after it is transmitted to a mammalian organism during a tick blood meal. B. burgdorferi encodes at least 140 lipoproteins located on the outer or inner membrane, thus facing the surroundings or the periplasmic space, respectively. However, most of the predicted lipoproteins are of unknown function, and only a few proteins are known to be essential for the persistence and virulence of the pathogen. One such protein is the periplasmic BB0323, which is indispensable for B. burgdorferi to cause Lyme disease and the function of which is associated with cell fission and outer membrane integrity. After expression and transport to the periplasm, BB0323 is cleaved into C-terminal and N-terminal domains by the periplasmic serine protease BB0104. The resulting N-terminal domain is sufficient to ensure the survival of B. burgdorferi throughout the mouse-tick infection cycle. The crystal structure of the N-terminal domain of BB0323 was determined at 2.35 A resolution. The overall fold of the protein belongs to the spectrin superfamily, with the characteristic interconnected triple-helical bundles known as spectrin repeats that function as linkers between different cell components in other organisms. Overall, the reported three-dimensional structure of the N-terminal domain of BB0323 not only reveals the molecular details of a protein that is essential for B. burgdorferi membrane integrity, cell fission and infectivity, but also suggests that spectrin repeats in bacteria are not limited to the EzrA proteins.
机译：莱姆病是一种感染造成的螺旋菌后伯氏疏螺旋体传输到哺乳动物有机体在蜱虫血粉。脂蛋白位于外部或内部膜,从而面临的环境或分别细胞周质间隙。预测的脂蛋白是未知的已知函数,只有少数蛋白质基本的持久性和毒性病原体。包柔氏螺旋体菌的BB0323,这是必不可少的。但是导致莱姆病和函数与细胞分裂和外膜的完整性。运输到周质,BB0323裂解c端和n端结构域周质的丝氨酸蛋白酶BB0104。n端结构域能充分保证b . burgdorferi整个的生存感染老鼠生命周期。BB0323 n端结构域的决心2.35一项决议。蛋白质属于血影蛋白总科,互联triple-helical特点包被称为血影蛋白功能的重复不同细胞之间的连接器组件其他生物。三维结构的n端域BB0323不仅揭示了分子细节是至关重要的一种蛋白质。burgdorferi膜完整性、细胞分裂和传染性,但也表明,血影蛋白重复在细菌并不局限于以斯拉蛋白质。

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