Institute for Animal Health, Pirbright Laboratory, Surrey, UK.
Traffic. 2012 Jan;13(1):30-42. doi: 10.1111/j.1600-0854.2011.01293.x. Epub 2011 Oct 24.
Infection of cells with African swine fever virus (ASFV) can lead to the formation of zipper-like stacks of structural proteins attached to collapsed endoplasmic reticulum (ER) cisternae. We show that the collapse of ER cisternae observed during ASFV infection is dependent on the viral envelope protein, J13Lp. Expression of J13Lp alone in cells is sufficient to induce collapsed ER cisternae. Collapse was dependent on a cysteine residue in the N-terminal domain of J13Lp exposed to the ER lumen. Luminal collapse was also dependent on the expression of J13Lp within stacks of ER where antiparallel interactions between the cytoplasmic domains of J13Lp orientated N-terminal domains across ER cisternae. Cisternal collapse was then driven by disulphide bonds between N-terminal domains arranged in antiparallel arrays across the ER lumen. This provides a novel mechanism for biogenesis of modified stacks of ER present in cells infected with ASFV, and may also be relevant to cellular processes.
非洲猪瘟病毒（ASFV）感染细胞可导致与折叠内质网（ER）池连接的结构蛋白形成拉链状堆叠。我们表明，在 ASFV 感染过程中观察到的 ER 池的折叠依赖于病毒包膜蛋白 J13Lp。单独在细胞中表达 J13Lp 足以诱导折叠的 ER 池。折叠依赖于 J13Lp 的 N 端结构域中的半胱氨酸残基暴露在 ER 腔中。腔的折叠还依赖于 J13Lp 在 ER 堆叠中的表达，其中 J13Lp 的细胞质结构域之间的反平行相互作用将 N 端结构域定向穿过 ER 池。然后，通过在 ER 腔中排列成反平行的二硫键驱动池的折叠。这为 ASFV 感染细胞中存在的修饰的 ER 堆叠的生物发生提供了一种新的机制，也可能与细胞过程有关。
