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Two Domains within the Mycoplasma hyopneumoniae Cilium Adhesin Bind Heparin

机译：猪肺炎支原体环黏附素结合肝素的两个结构域

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Mycoplasma hyopneumoniae is the causative agent of porcine enzootic pneumonia, a chronic and economically significant respiratory disease that affects swine production worldwide. M. hyopneumoniae adheres to and adversely affects the function of ciliated epithelial cells of the respiratory tract, and the cilium adhesin (Mhp183, P97) is intricately but not exclusively involved in this process. Although binding of pathogenic bacteria to glycosaminoglycans is a recognized step in pathogenesis, knowledge of glycosaminoglycan-binding proteins in M. hyopneumoniae is lacking. However, heparin and other sulfated polysaccharides are known to block the binding of M. hyopneumoniae to purified swine respiratory cilia. In this study, four regions within the cilium adhesin were examined for the ability to bind heparin. Cilium adhesin fragments comprising 653 amino acids of the N terminus and 301 amino acids of the C terminus (containing two repeat regions, R1 and R2) were cloned and expressed. These fragments bound heparin in a dose-dependent and saturable manner with physiologically significant binding affinities of 0.27 ± 0.02 μM and 1.89 ± 0.33 μM, respectively. Heparin binding of both fragments was strongly inhibited by the sulfated polysaccharides fucoidan and mucin but not by chondroitin sulfate B. When the C-terminal repeat regions R1 and R2 were cloned separately and expressed, heparin-binding activity was lost, suggesting that both regions are required for heparin binding. The ability of the cilium adhesin to bind heparin indicates that this molecule plays a multifunctional role in the adherence of M. hyopneumoniae to host respiratory surfaces and therefore has important implications with respect to the pathogenesis of this organism.
机译：猪肺炎支原体是猪流行性肺炎的病原体，这是一种慢性疾病，在经济上具有重要意义，影响着全世界的猪生产。 M。猪肺炎粘附并不利地影响了呼吸道纤毛上皮细胞的功能，纤毛粘附蛋白（Mhp183，P97）复杂但并非专门参与此过程。尽管病原菌与糖胺聚糖的结合是发病机理中公认的步骤，但了解糖蛋白在M中的结合。缺乏猪肺炎。但是，已知肝素和其他硫酸化的多糖会阻断 M的结合。猪肺炎至纯净的猪呼吸道纤毛。在这项研究中，检查纤毛粘附素内的四个区域结合肝素的能力。克隆并表达了包含N末端的653个氨基酸和C末端的301个氨基酸的Cilium粘附素片段（包含两个重复区域，R1和R2）。这些片段以剂量依赖性和饱和方式结合肝素，其生理学上显着的结合亲和力分别为0.27±0.02μM和1.89±0.33μM。硫酸多糖，岩藻依聚糖和粘蛋白强烈抑制两个片段的肝素结合，而硫酸软骨素B则不抑制。当C末端重复区域R1和R2分别克隆并表达时，肝素结合活性丧失，表明这两个区域都是肝素结合所需。纤毛粘附素结合肝素的能力表明该分子在 M的粘附中起多功能作用。肺炎链球菌可容纳呼吸道表面，因此对于这种生物的发病机理具有重要意义。

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