Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of Borrelia turicatae outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family.

中文翻译：

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伯氏疏螺旋体外表面脂蛋白 BBP28（mlp 蛋白家族成员）的溶液 NMR 结构

莱姆病是北美和欧洲最普遍的媒介传播疾病，由感染伯氏疏螺旋体复合螺旋体引起。我们报告了伯氏疏螺旋体外表面脂蛋白 BBP28的溶液核磁共振结构，它是多拷贝脂蛋白 (mlp) 家族的成员。该结构包含一个系链肽、五个 α 螺旋和一个延伸的 C 端环。该折叠类似于Borrelia turicatae外表面蛋白BTA121，已知其与脂质结合。这些结果通过揭示来自广泛发现的 mlp 家族的蛋白质的分子结构，有助于了解莱姆病的发病机制。