The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells.
The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells.
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DOI：
10.1371/journal.pone.0011301
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发表时间：
2010-06-24
期刊：
影响因子：
3.7
通讯作者：
Chang YF
中科院分区：
文献类型：
--
作者：
Lin YP;McDonough SP;Sharma Y;Chang YF
钩端螺旋体是引起人畜共患病钩端螺旋体病的致病螺旋体。钩端螺旋体免疫球蛋白(Ig)样蛋白B(LigB)参与钩端螺旋体与细胞外基质蛋白如纤维连接蛋白、纤维蛋白原、层粘连蛋白、弹性蛋白、原弹性蛋白和胶原的结合。LigB的高亲和力Fn结合区定位于LigBCen2，它包含LigB的部分第11和第12类Ig重复序列(LigBCen2R)和LigB非重复区域(LigBCen2NR)的47个氨基酸。在本研究中，纤维连接蛋白的明胶结合区与LigBCen2R相互作用(Kd = 为1.91±0.40µM)。不仅LigBCen2R，而且LigAVar7‘-8、LigAVar10、LigAVar11、LigAVar12、LigAVar13、LigBCen7’-8和LigBCen9等Lig蛋白的其他类Ig结构域也能与GBD结合。有趣的是，通过亲和力效应获得了很大的亲和力，与没有这种末端重复的重组蛋白相比，Lig蛋白的第13个(LIGA)或第12个(LigB)类Ig重复序列(LigAVar7‘-13和LigBCen7’-12)的结合亲和力分别提高了51倍和28倍。此外，带有末端结构域的Lig蛋白也可以促进对MDCKs细胞的抑制作用，但这两个结构域不是明胶结合域结合和细胞黏附所必需的。有趣的是，带有末端结构域的Lig蛋白可以在多结构域相互作用的作用下形成致密的圆形结构。这是关于FN和Lig蛋白的明胶结合域相互作用的首次报道，并提供了一个Lig-明胶结合域结合介导细菌-宿主相互作用的例子。
Leptospira spp. are pathogenic spirochetes that cause the zoonotic disease leptospirosis. Leptospiral immunoglobulin (Ig)-like protein B (LigB) contributes to the binding of Leptospira to extracellular matrix proteins such as fibronectin, fibrinogen, laminin, elastin, tropoelastin and collagen. A high-affinity Fn-binding region of LigB has been localized to LigBCen2, which contains the partial 11th and full 12th Ig-like repeats (LigBCen2R) and 47 amino acids of the non-repeat region (LigBCen2NR) of LigB. In this study, the gelatin binding domain of fibronectin was shown to interact with LigBCen2R (KD = 1.91±0.40 µM). Not only LigBCen2R but also other Ig-like domains of Lig proteins including LigAVar7'-8, LigAVar10, LigAVar11, LigAVar12, LigAVar13, LigBCen7'-8, and LigBCen9 bind to GBD. Interestingly, a large gain in affinity was achieved through an avidity effect, with the terminal domains, 13th (LigA) or 12th (LigB) Ig-like repeat of Lig protein (LigAVar7'-13 and LigBCen7'-12) enhancing binding affinity approximately 51 and 28 fold, respectively, compared to recombinant proteins without this terminal repeat. In addition, the inhibited effect on MDCKs cells can also be promoted by Lig proteins with terminal domains, but these two domains are not required for gelatin binding domain binding and cell adhesion. Interestingly, Lig proteins with the terminal domains could form compact structures with a round shape mediated by multidomain interaction. This is the first report about the interaction of gelatin binding domain of Fn and Lig proteins and provides an example of Lig-gelatin binding domain binding mediating bacterial-host interaction.
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影响因子：
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