A domain of the Leptospira LigB contributes to high affinity binding of fibronectin
A domain of the Leptospira LigB contributes to high affinity binding of fibronectin
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DOI：
10.1016/j.bbrc.2007.07.196
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发表时间：
2007-10-19
影响因子：
3.1
通讯作者：
Chang, Yung-Fu
中科院分区：
文献类型：
--
作者：
Lin, Yi-Pin;Chang, Yung-Fu
致病性钩端螺旋体的粘附。对哺乳动物细胞的作用是通过其粘附素与宿主细胞受体相互作用介导的。在之前的研究中，我们在致病性钩端螺旋体属粘附素 LigB 的中央可变区 (LigBCen) 和 C 末端可变区 (LigBCtv) 中确定了两个潜在的纤连蛋白 (Fn) 结合位点。在这项研究中，我们进一步定位了LigBCen上的Fn结合位点，并发现了LigB的结构域（LigBCen2）（氨基酸10 14-1165）与Fn强结合。 LigBCen2 与 Fn 的 70 kDa 结构域结合，包括 N 末端结构域 (NTD) 和明胶结合结构域 (GBD)，但与 NTD (K-d = 272 nM) 的结合亲和力高于与 GBD (Kd = 1200 nM) 的结合亲和力。除Fn外，LigBCen2还结合层粘连蛋白和纤维蛋白原。 LigBCen2可以结合MDCK细胞，并阻断钩端螺旋体对MDCK细胞的结合45%。这些结果表明，LigBCon2 有助于 Fn、层粘连蛋白和纤维蛋白原在 NTD 或 GBD 上的高亲和力结合，并介导钩端螺旋体与宿主细胞的结合。 (c) 2007 Elsevier Inc. 保留所有权利。
Adhesion of pathogenic Leplospira spp. to mammalian cells is mediated by their adhesins interacting with host cell receptors. In a previous study, we have identified two potential fibronectin (Fn) binding sites in central variable region (LigBCen) and C-terminal variable region (LigBCtv) of LigB, an adhesin of pathogenic Leptospira spp. In this study, we have further localized the Fn-binding site on LigBCen and found a domain of LigB (LigBCen2) (amino acids 10 14-1165) strongly bound to Fn. LigBCen2 bound to a 70 kDa domain of Fn including N-terminal domain (NTD) and gelatin binding domain (GBD), but with a higher binding affinity to NTD (K-d = 272 nM) than to GBD (Kd = 1200 nM). Except Fn, LigBCen2 also bound laminin and fibrinogen. LigBCen2 could bind MDCK cells, and blocked the binding of Leptospira on MDCK cells by 45%. These results suggest that LigBCon2 contributed to high affinity binding on NTD or GBD of Fn, laminin, and fibrinogen and mediated Leptospira binding on host cells. (c) 2007 Elsevier Inc. All rights reserved.