Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi
Crystal structure of Lyme disease antigen outer surface protein C from Borrelia burgdorferi
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DOI：
10.1074/jbc.m010062200
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发表时间：
2001-03-30
影响因子：
4.8
通讯作者：
Sacchettini, JC
中科院分区：
文献类型：
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作者：
Eicken, C;Sharma, V;Sacchettini, JC
外表面蛋白 C (OspC) 是伯氏疏螺旋体（莱姆病的病原体）的主要宿主诱导抗原之一。我们已经解析了重组 OspC 的晶体结构，分辨率为 2.5 埃。 OspC 是一种主要为 α 螺旋的蛋白质，是一种二聚体，具有特征性的中央四螺旋束，由每个亚基的两个最长螺旋连接而成。OspC 与 OspA 非常不同，但与细菌天冬氨酸受体的胞外结构域和来自布氏锥虫的变体表面糖蛋白相似。 OspC 在不同的 OspC 分离株之间差异很大。两个长α螺旋的膜近半部分是唯一可被溶剂接触的保守区域。由于重组 OspC 疫苗已被证明可以在小鼠中引发保护性免疫反应，因此这些区域是基于肽的疫苗的候选区域。
The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 Angstrom OspC, a largely alpha -helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit, OspC is very different from OspA and similar to the extracellular domain of the bacterial aspartate receptor and the variant surface glycoprotein from Trypanosoma brucei, Most of the surface-exposed residues of OspC are highly variable among different OspC isolates. The membrane proximal halves of the two long alpha -helices are the only conserved regions that are solvent accessible. As vaccination with recombinant OspC has been shown to elicit a protective immune response in mice, these regions are candidates for peptide-based vaccines.