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Translocation of Incoming Pseudorabies Virus Capsids to the Cell Nucleus Is Delayed in the Absence of Tegument Protein pUL37

机译:在缺乏皮层蛋白pUL37的情况下传入的伪狂犬病病毒衣壳向细胞核的易位延迟。

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摘要

After fusion of the envelope of herpesvirus particles with the host cell plasma membrane, incoming nucleocapsids are transported to nuclear pores. Inner tegument proteins pUL36, pUL37, and pUS3 remain attached to the nucleocapsid after entry and therefore might mediate interactions between the nucleocapsid and cellular microtubule-associated motor proteins during transport. To assay for the role of pUL37 in this process, we constructed a pUL37-deleted pseudorabies virus mutant, PrV-ΔUL37/UL35GFP, which expresses a fusion protein of green fluorescent protein (GFP) and the nonessential small capsid protein pUL35, resulting in the formation of fluorescently labeled capsids. Confocal laser-scanning microscopy of rabbit kidney cells infected with PrV-ΔUL37/UL35GFP revealed that, whereas penetration was not affected in the absence of pUL37, nuclear translocation of incoming particles was delayed by approximately 1 h compared to PrV-UL35GFP, but not abolished. In contrast, phenotypically complemented pUL37-containing virions of PrV-ΔUL37/UL35GFP exhibited wild type-like entry kinetics. Thus, the presence of pUL37 is required for rapid nuclear translocation of incoming nucleocapsids.
机译:疱疹病毒颗粒的包膜与宿主细胞质膜融合后,进入的核衣壳被转运至核孔。内皮蛋白pUL36,pUL37和pUS3进入后仍保持附着于核衣壳,因此可能在转运过程中介导核衣壳与细胞微管相关运动蛋白之间的相互作用。为了测定pUL37在此过程中的作用,我们构建了一个pUL37缺失的伪狂犬病病毒突变体PrV-ΔUL37/ UL35GFP,它表达绿色荧光蛋白(GFP)和非必需小衣壳蛋白pUL35的融合蛋白,荧光标记衣壳的形成。通过共聚焦激光扫描显微镜观察感染了PrV-ΔUL37/ UL35GFP的兔肾细胞,尽管在不存在pUL37的情况下穿透不受影响,但与PrV-UL35GFP相比,进入颗粒的核转运延迟了大约1小时,但并未取消。相反,PrV-ΔUL37/ UL35GFP的表型互补的含pUL37的病毒粒子表现出类似野生型的进入动力学。因此,pUL37的存在是传入核衣壳快速核转运所需的。

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