Merien F, Truccolo J, Baranton G, Perolat P
Leptospira Laboratory, Institut Pasteur de Nouvelle-Calédonie, P.O. Box 61, 98845, Nouméa, New Caledonia.
FEMS Microbiol Lett. 2000 Apr 1;185(1):17-22. doi: 10.1111/j.1574-6968.2000.tb09034.x.
We investigated the ability of a virulent strain of Leptospira interrogans serovar icterohaemorrhagiae, its isogenic avirulent variant and a saprophytic strain to bind fibronectin using alkaline phosphatase-labelled fibronectin. A single 36-kDa fibronectin-binding protein was expressed only by the virulent strain and was located in the outer sheath according to proteinase K treatment results. The interaction of this protein with fibronectin was specific and the region of fibronectin bound to this potential adhesin overlapped the gelatin-binding domain. The inability of a RGDS synthetic peptide to inhibit the binding of fibronectin indicated that the cell-binding domain was not involved in this interaction. Considering the wide distribution of fibronectin within a host and the diversity of mammals involved in the epidemiology of leptospirosis, its implication in the cell attachment process of virulent leptospires is coherent with the multiplicity of target cells.
我们使用碱性磷酸酶标记的纤连蛋白，研究了问号钩端螺旋体黄疸出血血清型的强毒株、其同基因无毒变种以及腐生菌株结合纤连蛋白的能力。仅强毒株表达一种单一的36 kDa纤连蛋白结合蛋白，根据蛋白酶K处理结果，该蛋白位于外鞘中。该蛋白与纤连蛋白的相互作用具有特异性，与这种潜在粘附素结合的纤连蛋白区域与明胶结合域重叠。RGDS合成肽无法抑制纤连蛋白的结合，表明细胞结合域不参与这种相互作用。考虑到纤连蛋白在宿主体内广泛分布以及钩端螺旋体病流行病学涉及的哺乳动物种类多样，其在强毒钩端螺旋体细胞附着过程中的作用与靶细胞的多样性是一致的。
