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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of an outer surface lipoprotein BBA64 from the Lyme disease agent Borrelia burgdorferi which is critical to ensure infection after a tick bite
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Structure of an outer surface lipoprotein BBA64 from the Lyme disease agent Borrelia burgdorferi which is critical to ensure infection after a tick bite

机译：脂蛋白BBA64外表面的结构从莱姆病代理。伯氏疏螺旋体确保后感染的关键是什么蜱虫咬

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摘要

Lyme disease is a tick-borne infection caused by the transmission of Borrelia burgdorferi from infected Ixodes ticks to a mammalian host during the blood meal. Previous studies have shown that the expression of B. burgdorferi surface-localized lipoproteins, which include BBA64, is up-regulated during the process of tick feeding. Although the exact function of BBA64 is not known, this lipoprotein is critical for the transmission of the spirochete from the tick salivary glands to the mammalian organism after a tick bite. Since the mechanism of development of the disease and the functions of the surface lipoproteins associated with borreliosis are still poorly understood, the crystal structure of the B. burgdorferi outer surface lipoprotein BBA64 was solved at 2.4 14;? resolution in order to obtain a better insight into the pathogenesis of B. burgdorferi and to promote the discovery of novel potential preventive drugs against Lyme disease. In this study, the crystal structure of BBA64 was also compared with that of the paralogous protein CspA (also referred to as BbCRASP-1, CRASP-1 or BBA68). CspA is the complement regulator-acquiring surface protein-1 of B. burgdorferi; its structure is known, but its function apparently differs from that of BBA64. It is demonstrated that unlike the homologous CspA, BBA64 does not form a homodimer. Their differences in function could be explained by divergence in their amino-acid sequences, electrostatic surface potentials and overall tertiary structures. The C-terminal part of BBA64 has a different conformation to that of CspA; the conformation of this region is essential for the proper function of CspA.
机译：莱姆病是一种蜱传播的感染所致从伯氏疏螺旋体的传播感染Ixodes蜱虫在哺乳动物宿主血粉。b . burgdorferi的表达surface-localized脂蛋白,包括BBA64,上调过程中喂食。不知道,这脂蛋白是至关重要的蜱虫的螺旋菌的传播唾液腺后哺乳动物有机体蜱虫咬人。疾病和表面的功能与莱姆疏螺旋体病相关的脂蛋白仍然知之甚少,的晶体结构b . burgdorferi外表面脂蛋白在2.4 14;BBA64解决了吗?获得更好的洞察发病机理b . burgdorferi和促进的发现小说的潜在对莱姆预防性药物疾病。BBA64也相比的paralogous蛋白质CspA(也称为BbCRASP-1 CRASP-1或BBA68)。补充regulator-acquiring表面蛋白1b . burgdorferi;它的功能显然是不同的BBA64。为同源CspA BBA64不形式。他们的差异可以解释功能散度的氨基酸序列,表面静电势和整体三级结构。有不同的构象CspA;本地区的构象是必不可少的适当的CspA的函数。

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