Department of Veterinary Pathobiology, College of Veterinary Medicine and Biomedical Sciences, Texas A&M University, College Station, Texas, USA.
J Bacteriol. 2013 Aug;195(15):3320-30. doi: 10.1128/JB.00187-13. Epub 2013 May 17.
Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal membranes and with detergent phase separation assays. Our results showed evidence of BB0172 localization in the outer membrane, the orientation of the vWFA domain to the extracellular environment, and its function as a metal ion-dependent integrin-binding protein. This is the first report of a borrelial adhesin with a metal ion-dependent adhesion site (MIDAS) motif that is similar to those observed in eukaryotic integrins and has a similar function.
莱姆病是一种由伯氏疏螺旋体感染引起的多系统疾病。感染后,一些伯氏疏螺旋体基因上调,包括微生物表面成分识别黏附基质分子(MSCRAMM)蛋白家族的成员,这些蛋白有助于伯氏疏螺旋体黏附到宿主细胞外基质成分上。比较基因组分析揭示了伯氏疏螺旋体蛋白的一个新家族,其中包含血管性血友病因子 A(vWFA)结构域。在本研究中,我们通过体外转录/翻译系统,在微粒体膜存在的情况下,以及通过去污剂相分离实验,对含有 vWFA 结构域的蛋白 BB0172 的表达和膜结合特性进行了表征。我们的结果表明,BB0172 定位于外膜,vWFA 结构域朝向细胞外环境,并且作为金属离子依赖性整合素结合蛋白发挥功能。这是首例报道具有类似于真核整合素的金属离子依赖性黏附位点(MIDAS)基序的螺旋体黏附素,并且具有相似的功能。