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首页> 外文期刊>Journal of Receptor, Ligand and Channel Research >Pentameric viral ion channels: from structure to function
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Pentameric viral ion channels: from structure to function

机译：五聚体病毒离子通道：从结构到功能

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Abstract: A family of small polypeptides in many virus types associate to form oligomers and have channel activity. These proteins have been referred to as viroporins or virochannels and are increasingly recognized as important virulence factors and potential drug targets. In this review, we focus on two of the viroporins that have been studied in more detail from a structural and functional point of view. One is the 76-residue envelope (E) protein found in coronaviruses (CoVs) that causes the severe acute respiratory syndrome (SARS). The other is the 65-residue small hydrophobic (SH) protein found in a paramyxovirus, the respiratory syncytial virus (RSV). RSV SH and SARS-CoV E proteins are short polypeptides with a single transmembrane domain. In both cases, the presence of the viroporin has a protective effect on cells, preventing early apoptosis, but it leads to increased virulence in infected animal models. Both viroporins form homopentameric oligomers that show channel activity with no or low selectivity. The role of channel activity is still unclear, but associations have been made to facilitation of the egress of the virus by modification of the secretory pathway, and contributions to inflammation. SARS-CoV E protein has a cytoplasmically oriented C-terminus and a lumenal N-terminus, whereas the opposite orientation is found in RSV SH protein. Despite this opposite topology, nuclear magnetic resonance (NMR)-based structural models of these two channels show a similar champagne flute shape, with the wider opening facing the cytoplasmic side. Good channel inhibitors are lacking, but those found seem to have a preference for the narrow end of the channel. Availability of good inhibitors will help reveal the specific role of these channels in the life cycle of these viruses.
机译：摘要：许多病毒类型的小型多肽家族缔合形成寡聚物并具有通道活性。这些蛋白质被称为viroporin或病毒通道，并日益被认为是重要的毒力因子和潜在的药物靶标。在这篇综述中，我们着重从结构和功能的角度对两种维罗蛋白进行了更详细的研究。一种是在冠状病毒（CoV）中发现的76个残留的包膜（E）蛋白，可导致严重的急性呼吸道综合症（SARS）。另一个是在副粘病毒，呼吸道合胞病毒（RSV）中发现的具有65个残基的小疏水（SH）蛋白。 RSV SH和SARS-CoV E蛋白是具有单个跨膜结构域的短多肽。在这两种情况下，维罗帕林的存在对细胞都有保护作用，可防止早期凋亡，但会导致感染动物模型的毒力增加。两种维罗帕林均形成均五聚体低聚物，其显示通道活性而没有或具有低选择性。通道活性的作用仍不清楚，但是已经通过改变分泌途径和促进炎症来促进病毒的释放。 SARS-CoV E蛋白具有细胞质定向的C末端和内腔N末端，而RSV SH蛋白质则具有相反的定向。尽管存在这种相反的拓扑结构，但这两个通道的基于核磁共振（NMR）的结构模型仍显示出类似的香槟槽形状，且较宽的开口面向细胞质侧。缺少好的通道抑制剂，但是发现的通道抑制剂似乎更喜欢通道的狭窄末端。好的抑制剂的可用性将有助于揭示这些通道在这些病毒的生命周期中的特定作用。

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