Borrelia burgdorferi BmpA Is a Laminin-Binding Protein
Borrelia burgdorferi BmpA Is a Laminin-Binding Protein
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DOI：
10.1128/iai.01420-08
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发表时间：
2009-11-01
影响因子：
3.1
通讯作者：
Stevenson, Brian
中科院分区：
文献类型：
--
作者：
Verma, Ashutosh;Brissette, Catherine A.;Stevenson, Brian
伯氏疏螺旋体BmpA外表面蛋白在哺乳动物莱姆病螺旋体感染中起重要作用，是人类感染的重要血清诊断抗原。伯氏疏螺旋体附着在宿主细胞外基质成分上，包括层粘连蛋白。我们的研究结果表明，BmpA及其三个同源蛋白BmpB、BmpC和BmpD都与哺乳动物层粘连蛋白结合。BmpA不与哺乳动物I型或IV型胶原或纤维连接蛋白结合。bmpa定向抗体显著抑制活伯氏疏螺旋体对层粘连蛋白的粘附。BmpA的层粘连蛋白结合结构域被定位到羧基端80个氨基酸。溶解的胶原抑制了bmpa -层粘连蛋白的结合，表明通过层粘连蛋白的胶原结合结构域相互作用。这些结果与先前的数据一起表明，BmpA及其类似物是开发莱姆病预防和治疗疗法的目标。
The Borrelia burgdorferi BmpA outer surface protein plays a significant role in mammalian infection by the Lyme disease spirochete and is an important antigen for the serodiagnosis of human infection. B. burgdorferi adheres to host extracellular matrix components, including laminin. The results of our studies indicate that BmpA and its three paralogous proteins, BmpB, BmpC, and BmpD, all bind to mammalian laminin. BmpA did not bind mammalian type I or type IV collagens or fibronectin. BmpA-directed antibodies significantly inhibited the adherence of live B. burgdorferi to laminin. The laminin- binding domain of BmpA was mapped to the carboxy-terminal 80 amino acids. Solubilized collagen inhibited BmpA-laminin binding, suggesting interactions through the collagen-binding domains of laminin. These results, together with previous data, indicate that BmpA and its paralogs are targets for the development of preventative and curative therapies for Lyme disease.