Binding of Bartonella henselae to extracellular molecules: Identification of potential adhesins
Binding of Bartonella henselae to extracellular molecules: Identification of potential adhesins
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DOI：
10.1016/j.micpath.2006.04.003
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发表时间：
2006-07-01
影响因子：
3.8
通讯作者：
Anderson, B. E.
中科院分区：
文献类型：
--
作者：
Dabo, S. M.;Confer, A. W.;Anderson, B. E.
亨塞巴尔通体是猫抓病、细菌性血管瘤病和其他临床综合征的病原体，通过皮肤创伤或伤口引发感染，表明细胞外基质分子参与其中。在这项研究中，我们已经证明，B. henselae结合纤维连接蛋白、胶原IX和X很强，而层粘连蛋白和胶原IV相对较少。B. henselae主要结合N端和c端肝素（分别为Hep-1和Hep-2）和纤维连接蛋白的明胶结合域（Fn），而不是细胞结合域。Hep显著抑制了与Hep结合域的结合，提示Fn分子上有共同的结合位点。此外，糖胺聚糖介导的B. henselae与可溶性Fn的结合表明，Hep而不是葡聚糖硫酸盐抑制了细菌与Fn的结合。与Fn不同的是，只有在Hep或硫酸葡聚糖存在时，B. henselae才能与玻璃体粘连蛋白结合。此外，抗b抗体还能抑制蜜蜂与宿主细胞的结合。鸡翅表面反应性抗体，外源性Fn或抗Fn多克隆抗体。配体印迹、批量亲和纯化和MALDI-TOF肽指纹图谱鉴定了母鸡B. B.鸡翅外膜蛋白中三个主要的fn结合蛋白（FnBPs），分别为Pap31、Omp43和Omp89。我们假设亨selae伤口相关感染与细胞外基质分子相互作用有关。综上所述，上述数据表明，B. henselae与Fn等ECM分子的相互作用可能在细菌粘附和侵袭宿主细胞中起重要作用。(c) 2006 Elsevier Ltd.版权所有。
Bartonella henselae, the etiologic agent of cat scratch disease, bacillary angiomatosis and other clinical syndromes initiates infection through a trauma or wound to the skin suggesting involvement of extracellular matrix molecules. We have demonstrated in this study that B. henselae bound strongly fibronectin, collagen IX and X, but comparatively less laminin and collagen IV. B. henselae bound primarily the N- and C-terminal heparin (Hep-1 and Hep-2, respectively) and the gelatin-binding domains of fibronectin (Fn) but not the cell-binding domain. Binding to the Hep-binding domain was significantly inhibited by Hep suggesting common binding sites on the Fn molecule. Furthermore, glycosaminoglycans-mediated binding of B. henselae to soluble Fn showed that Hep but not dextran sulfate inhibited the bacterium binding to Fn. Unlike Fn, B. henselae bound strongly vitronectin only in the presence of Hep or dextran sulfate. Also, the binding of B. henselae to host cells could be inhibited by anti-B. henselae surface-reactive antibodies, the exogenous Fn or the anti-Fn polyclonal antibodies. Ligand blots, batch affinity purification and MALDI-TOF peptide fingerprinting identified B. henselae Pap31, Omp43 and Omp89 as the three major putative Fn-binding proteins (FnBPs) in B. henselae outer membrane proteins. We hypothesized that B. henselae Wound associated infections involved interactions with extracellular matrix molecules. Taken together, the above data suggest that interactions between B. henselae and ECM molecules such as Fn may play an important role in the bacterium adherence to and invasion of host cells. (c) 2006 Elsevier Ltd. All rights reserved.