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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain
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Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain

机译：幽门螺杆菌空泡毒素p55域的晶体结构

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摘要

Helicobacter pylori VacA, a pore-forming toxin secreted by an autotransporter pathway, causes multiple alterations in human cells, contributes to the pathogenesis of peptic ulcer disease and gastric cancer, and is a candidate antigen for inclusion in an H. pylori vaccine. Here, we present a 2.4-A crystal structure of the VacA p55 domain, which has an important role in mediating VacA binding to host cells. The structure is predominantly a right-handed parallel β-helix, a feature that is characteristic of autotransporter passenger domains but unique among known bacterial protein toxins. Notable features of VacA p55 include disruptions in β-sheet contacts that result in five β-helix subdomains and a C-terminal domain that contains a disulfide bond. Analysis of VacA protein sequences from unrelated H. pylori strains, including ml and m2 forms of VacA, allows us to identify structural features of the VacA surface that may be important for interactions with host receptors. Docking of the p55 structure into a 19-A cryo-EM map of a VacA dodecamer allows us to propose a model for how VacA monomers assemble into oligomeric structures capable of membrane channel formation.
机译：幽门螺杆菌VacA是一种由自转运蛋白途径分泌的成孔毒素，会引起人体细胞的多种变化，导致消化性溃疡和胃癌的发病机理，并且是包含在幽门螺杆菌疫苗中的候选抗原。在这里，我们介绍了VacA p55域的2.4-A晶体结构，在介导VacA与宿主细胞的结合中具有重要作用。该结构主要是右手平行的β-螺旋，该特征是自转运体乘客结构域的特征，但在已知的细菌蛋白毒素中却是独特的。 VacA p55的显着特征包括β-折叠接触的破坏，导致五个β-螺旋亚结构域和一个包含二硫键的C末端结构域。分析无关的幽门螺杆菌菌株的VacA蛋白序列，包括ml和m2形式的VacA，使我们能够鉴定VacA表面的结构特征，这可能对与宿主受体的相互作用很重要。将p55结构对接到VacA dodecamer的19-A冷冻EM图中，我们可以提出一个模型，用于VacA单体如何组装成能够形成膜通道的低聚结构。

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