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首页> 外文OA文献 >Functional Comparison of the Binding of Factor H Short Consensus Repeat 6 (SCR 6) to Factor H Binding Protein from Neisseria meningitidis and the Binding of Factor H SCR 18 to 20 to Neisseria gonorrhoeae Porin▿ †
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Functional Comparison of the Binding of Factor H Short Consensus Repeat 6 (SCR 6) to Factor H Binding Protein from Neisseria meningitidis and the Binding of Factor H SCR 18 to 20 to Neisseria gonorrhoeae Porin▿ †

机译：因子H短暂共有重复序列6（SCR 6）与脑膜炎奈瑟氏球菌因子H结合蛋白的结合以及因子H SCR 18-20与淋病奈瑟氏菌结合的功能比较†

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Both Neisseria meningitidis and Neisseria gonorrhoeae recruit the alternative pathway complement inhibitory protein factor H (fH) to their surfaces to evade complement-dependent killing. Meningococci bind fH via fH binding protein (fHbp), a surface-exposed lipoprotein that is subdivided into three variant families based on one classification scheme. Chimeric proteins that comprise contiguous domains of fH fused to murine Fc were used to localize the binding site for all three fHbp variants on fH to short consensus repeat 6 (SCR 6). As expected, fH-like protein 1 (FHL-1), which contains fH SCR 6, also bound to fHbp-expressing meningococci. Using site-directed mutagenesis, we identified histidine 337 and histidine 371 in SCR 6 as important for binding to fHbp. These findings may provide the molecular basis for recent observations that demonstrated human-specific fH binding to meningococci. Differences in the interactions of fHbp variants with SCR 6 were evident. Gonococci bind fH via their porin (Por) molecules (PorB.1A or PorB.1B); sialylation of lipooligosaccharide enhances fH binding. Both sialylated PorB.1B- and (unsialylated) PorB.1A-bearing gonococci bind fH through SCR 18 to 20; PorB.1A can also bind SCR 6, but only weakly, as evidenced by a low level of binding of FHL-1 relative to that of fH. Using isogenic strains expressing either meningococcal fHbp or gonococcal PorB.1B, we discovered that strains expressing gonococcal PorB.1B in the presence of sialylated lipooligosaccharide bound more fH, more effectively limited C3 deposition, and were more serum resistant than their isogenic counterparts expressing fHbp. Differences in fH binding to these two related pathogens may be important for modulating their individual responses to host immune attack.
机译：脑膜炎奈瑟氏球菌和淋病奈瑟氏球菌都向其表面募集了替代途径补体抑制蛋白因子H（fH），以逃避补体依赖性杀伤。脑膜炎球菌通过fH结合蛋白（fHbp）结合fH，fH结合蛋白是一种表面暴露的脂蛋白，根据一种分类方案分为三个变异家族。包含与鼠Fc融合的fH连续域的嵌合蛋白用于将fH上所有三个fHbp变体的结合位点定位在短共有重复序列6（SCR 6）上。不出所料，含有fH SCR 6的fH样蛋白1（FHL-1）也与表达fHbp的脑膜炎球菌结合。使用定点诱变，我们确定了SCR 6中的组氨酸337和组氨酸371对于结合fHbp很重要。这些发现可能为最近的发现提供分子基础，这些发现表明了人类特异性fH与脑膜炎球菌的结合。 fHbp变体与SCR 6相互作用的差异很明显。淋病球菌通过其孔蛋白（Por）分子（PorB.1A或PorB.1B）与fH结合；脂寡糖的唾液酸化增强fH结合。唾液酸化的PorB.1B和携带（未唾液酸化的）PorB.1A的淋球菌都通过SCR 18至20结合fH。 PorB.1A还可以与SCR 6结合，但只能与SCR 6结合，这由FHL-1相对于fH的结合水平低证明。使用表达脑膜炎球菌fHbp或淋球菌PorB.1B的同基因菌株，我们发现在存在唾液酸化低聚寡糖的情况下表达淋球菌PorB.1B的菌株结合了更多的fH，更有效地限制了C3的沉积，并且比表达fHbp的同基因菌株具有更高的血清耐药性。 fH与这两种相关病原体结合的差异对于调节它们对宿主免疫攻击的个体应答可能很重要。

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