The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin
The N-terminal A domain of fibronectin-binding proteins A and B promotes adhesion of Staphylococcus aureus to elastin
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DOI：
10.1074/jbc.m402122200
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发表时间：
2004-09-10
影响因子：
4.8
通讯作者：
Foster, TJ
中科院分区：
文献类型：
--
作者：
Roche, FM;Downer, R;Foster, TJ
金黄色葡萄球菌粘附于细胞外基质组分的能力是感染期间宿主组织定殖的重要机制。我们以前已经证明了S。金黄色葡萄球菌结合弹性蛋白，弹性蛋白是细胞外基质的主要成分。弹性蛋白结合蛋白（EbpS）是膜蛋白的一种，通过其表面暴露的N-末端结构域与可溶性弹性蛋白肽和弹性蛋白原结合。在这项研究中，我们证明了一些菌株的S。金黄色葡萄球菌强烈粘附于固定化的人弹性蛋白，并且这种相互作用不依赖于EbpS，而是由纤连蛋白结合蛋白FnBPA和FnBPB介导。我们的结果表明，EbpS突变细胞粘附弹性蛋白包被的板，而FnBPA和FnBPB阴性的细胞不粘附板。此外，只有野生型细胞的生长指数期时，粘附FnBP最大限度地表达。我们表明，FnBPA促进的弹性蛋白粘附不受可溶性纤连蛋白的影响，这表明弹性蛋白结合结构域与纤连蛋白结合区域不同。对应于FnBPA的A区的重组FnBPA（37 - 544）（rFnBPA（37-544））蛋白和抗FnBPA（37-544）抗体抑制FnBPA介导的细菌对固定化弹性蛋白的粘附。最后，重组A结构域蛋白rFnBPA（37-544）和rFnBPB（37-540）以剂量依赖性和饱和性结合固定的弹性蛋白。这种相互作用被可溶性弹性蛋白肽抑制，表明特异性受体-配体相互作用。
The ability of Staphylococcus aureus to adhere to components of the extracellular matrix is an important mechanism for colonization of host tissues during infection. We have previously shown that S. aureus binds elastin, a major component of the extracellular matrix. The integral membrane protein, elastin-binding protein (EbpS), binds soluble elastin peptides and tropoelastin via its surface-exposed N-terminal domain. In this study, we demonstrate that some strains of S. aureus adhere strongly to immobilized human elastin and that this interaction is independent of EbpS but instead is mediated by the fibronectin-binding proteins, FnBPA and FnBPB. Our results show that EbpS mutant cells adhere to elastin-coated plates, whereas the cells negative for FnBPA and FnBPB do not adhere to the plates. Furthermore, only wild-type cells from the exponential phase of growth adhered when FnBPs were expressed maximally. We show that adherence to elastin promoted by FnBPA was not affected by soluble fibronectin, suggesting that the elastin binding domain is distinct from the fibronectin binding regions. Recombinant FnBPA(37-544) (rFnBPA(37-544)) protein corresponding to the A region of FnBPA and anti-FnBPA(37-544) antibodies inhibited FnBPA-mediated bacterial adherence to immobilized elastin. Finally, recombinant A domain proteins, rFnBPA(37-544) and rFnBPB(37-540), bound immobilized elastin dose-dependently and saturably. This interaction was inhibited by soluble elastin peptides, suggesting a specific receptor-ligand interaction.