Department of Internal Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA.
PLoS Pathog. 2010 Sep 2;6(9):e1001087. doi: 10.1371/journal.ppat.1001087.
The hepatitis C virus (HCV) p7 protein is critical for virus production and an attractive antiviral target. p7 is an ion channel when reconstituted in artificial lipid bilayers, but channel function has not been demonstrated in vivo and it is unknown whether p7 channel activity plays a critical role in virus production. To evaluate the contribution of p7 to organelle pH regulation and virus production, we incorporated a fluorescent pH sensor within native, intracellular vesicles in the presence or absence of p7 expression. p7 increased proton (H(+)) conductance in vesicles and was able to rapidly equilibrate H(+) gradients. This conductance was blocked by the viroporin inhibitors amantadine, rimantadine and hexamethylene amiloride. Fluorescence microscopy using pH indicators in live cells showed that both HCV infection and expression of p7 from replicon RNAs reduced the number of highly acidic (pH<5) vesicles and increased lysosomal pH from 4.5 to 6.0. These effects were not present in uninfected cells, sub-genomic replicon cells not expressing p7, or cells electroporated with viral RNA containing a channel-inactive p7 point mutation. The acidification inhibitor, bafilomycin A1, partially restored virus production to cells electroporated with viral RNA containing the channel inactive mutation, yet did not in cells containing p7-deleted RNA. Expression of influenza M2 protein also complemented the p7 mutant, confirming a requirement for H(+) channel activity in virus production. Accordingly, exposure to acid pH rendered intracellular HCV particles non-infectious, whereas the infectivity of extracellular virions was acid stable and unaffected by incubation at low pH, further demonstrating a key requirement for p7-induced loss of acidification. We conclude that p7 functions as a H(+) permeation pathway, acting to prevent acidification in otherwise acidic intracellular compartments. This loss of acidification is required for productive HCV infection, possibly through protecting nascent virus particles during an as yet uncharacterized maturation process.
丙型肝炎病毒 (HCV) p7 蛋白对于病毒的产生至关重要,是一个有吸引力的抗病毒靶点。p7 在人工脂质双层中重新构建时是一种离子通道,但尚未在体内证明其通道功能,也不知道 p7 通道活性是否在病毒产生中起关键作用。为了评估 p7 对细胞器 pH 调节和病毒产生的贡献,我们在存在或不存在 p7 表达的情况下,将荧光 pH 传感器掺入到天然的细胞内囊泡中。p7 增加了囊泡中的质子 (H+) 传导能力,并能够快速平衡 H+梯度。这种传导能力被病毒蛋白抑制剂金刚烷胺、金刚乙胺和六亚甲基阿米洛利阻断。使用活细胞中的 pH 指示剂进行荧光显微镜检查表明,HCV 感染和来自复制子 RNA 的 p7 表达均降低了高度酸性(pH<5)囊泡的数量,并将溶酶体 pH 从 4.5 增加到 6.0。这些效应在未感染的细胞、不表达 p7 的亚基因组复制子细胞或用包含无通道活性 p7 点突变的病毒 RNA 转染的细胞中不存在。酸化抑制剂巴弗洛霉素 A1 部分恢复了用包含无通道活性突变的病毒 RNA 转染的细胞中的病毒产生,但在含有 p7 缺失 RNA 的细胞中则没有。流感 M2 蛋白的表达也补充了 p7 突变体,证实了 H+通道活性在病毒产生中的必要性。因此,暴露于酸性 pH 会使细胞内 HCV 颗粒失去感染性,而细胞外病毒粒子的感染性在酸性 pH 下稳定且不受低 pH 孵育的影响,进一步证明 p7 诱导的酸化损失是病毒产生所必需的。我们得出结论,p7 作为 H+渗透途径发挥作用,防止其他酸性细胞内隔室酸化。这种酸化的丧失是 HCV 感染有活力所必需的,可能是通过在尚未描述的成熟过程中保护新生病毒颗粒。