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首页> 美国卫生研究院文献>PLoS Pathogens >A lipid-binding loop of botulinum neurotoxin serotypes B DC and G is an essential feature to confer their exquisite potency
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A lipid-binding loop of botulinum neurotoxin serotypes B DC and G is an essential feature to confer their exquisite potency

机译：肉毒杆菌神经毒素血清型BDC和G的脂质结合环是赋予其精湛功效的基本特征

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摘要

The exceptional toxicity of botulinum neurotoxins (BoNTs) is mediated by high avidity binding to complex polysialogangliosides and intraluminal segments of synaptic vesicle proteins embedded in the presynaptic membrane. One peculiarity is an exposed hydrophobic loop in the toxin’s cell binding domain HC, which is located between the ganglioside- and protein receptor-binding sites, and that is particularly pronounced in the serotypes BoNT/B, DC, and G sharing synaptotagmin as protein receptor. Here, we provide evidence that this HC loop is a critical component of their tripartite receptor recognition complex. Binding to nanodisc-embedded receptors and toxicity were virtually abolished in BoNT mutants lacking residues at the tip of the HC loop. Surface plasmon resonance experiments revealed that only insertion of the HC loop into the lipid-bilayer compensates for the entropic penalty inflicted by the dual-receptor binding. Our results represent a new paradigm of how BoNT/B, DC, and G employ ternary interactions with a protein, ganglioside, and lipids to mediate their extraordinary neurotoxicity.
机译：肉毒杆菌神经毒素（BoNTs）的特殊毒性是通过高亲和力结合到复杂的多唾液酸神经节苷脂和嵌入突触前膜的突触小泡蛋白的腔内区段而介导的。一个特殊之处是毒素的细胞结合结构域HC中一个暴露的疏水环，该环位于神经节苷脂和蛋白质受体结合位点之间，并且在血清型BoNT / B，DC和G中以突触结合蛋白作为蛋白质受体而特别明显。在这里，我们提供的证据表明，该HC环是其三重受体识别复合物的关键组成部分。实际上，在HC环末端缺少残基的BoNT突变体中，与纳米盘嵌入受体的结合和毒性实际上被消除了。表面等离振子共振实验表明，仅将HC环插入脂质双层即可补偿双受体结合所造成的熵损失。我们的结果代表了BoNT / B，DC和G如何利用与蛋白质，神经节苷脂和脂质的三元相互作用来介导其非同寻常的神经毒性的新范例。

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