Department of Microbiology and Immunology, Center for Molecular and Tumor Virology, Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, Louisiana, United States of America.
Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, United States of America.
PLoS Pathog. 2019 Feb 25;15(2):e1007590. doi: 10.1371/journal.ppat.1007590. eCollection 2019 Feb.
Subnuclear promyelocytic leukemia (PML) nuclear bodies (NBs) are targeted by many DNA viruses after nuclear delivery. PML protein is essential for formation of PML NBs. Sp100 and Small Ubiquitin-Like Modifier (SUMO) are also permanently residing within PML NBs. Often, large DNA viruses disassemble and reorganize PML NBs to counteract their intrinsic antiviral activity and support establishment of infection. However, human papillomavirus (HPV) requires PML protein to retain incoming viral DNA in the nucleus for subsequent efficient transcription. In contrast, Sp100 was identified as a restriction factor for HPV. These findings suggested that PML NBs are important regulators of early stages of the HPV life cycle. Nuclear delivery of incoming HPV DNA requires mitosis. Viral particles are retained within membrane-bound transport vesicles throughout mitosis. The viral genome is released from transport vesicles by an unknown mechanism several hours after nuclear envelope reformation. The minor capsid protein L2 mediates intracellular transport by becoming transmembranous in the endocytic compartment. Herein, we tested our hypothesis that PML protein is recruited to incoming viral genome prior to egress from transport vesicles. High-resolution microscopy revealed that PML protein, SUMO-1, and Sp100 are recruited to incoming viral genomes, rather than viral genomes being targeted to preformed PML NBs. Differential immunofluorescent staining suggested that PML protein and SUMO-1 associated with transport vesicles containing viral particles prior to egress, implying that recruitment is likely mediated by L2 protein. In contrast, Sp100 recruitment to HPV-harboring PML NBs occurred after release of viral genomes from transport vesicles. The delayed recruitment of Sp100 is specific for HPV-associated PML NBs. These data suggest that the virus continuously resides within a protective environment until the transport vesicle breaks down in late G1 phase and imply that HPV might modulate PML NB assembly to achieve establishment of infection and the shift to viral maintenance.
亚核早幼粒细胞白血病 (PML) 核体 (NB) 在核内运输后成为许多 DNA 病毒的靶标。PML 蛋白对于 PML NB 的形成至关重要。Sp100 和小泛素样修饰物 (SUMO) 也永久驻留在 PML NB 内。通常,大型 DNA 病毒会解体和重组 PML NB,以抵消其内在的抗病毒活性并支持感染的建立。然而,人乳头瘤病毒 (HPV) 需要 PML 蛋白将传入的病毒 DNA保留在核内,以随后进行有效的转录。相比之下,Sp100 被鉴定为 HPV 的限制因子。这些发现表明 PML NB 是 HPV 生命周期早期阶段的重要调节剂。传入 HPV DNA 的核内运输需要有丝分裂。病毒颗粒在整个有丝分裂过程中保留在膜结合的运输小泡内。病毒基因组通过未知机制在核膜重新形成后数小时从运输小泡中释放出来。次要衣壳蛋白 L2 通过在胞吞小体中成为跨膜蛋白来介导细胞内运输。在此,我们测试了我们的假设,即在从运输小泡中逸出之前,PML 蛋白被招募到传入的病毒基因组上。高分辨率显微镜显示,PML 蛋白、SUMO-1 和 Sp100 被招募到传入的病毒基因组上,而不是病毒基因组被靶向到预先形成的 PML NB 上。差示免疫荧光染色表明,PML 蛋白和 SUMO-1 在从运输小泡中逸出之前与含有病毒颗粒的运输小泡相关联,这意味着募集可能由 L2 蛋白介导。相比之下,Sp100 向 HPV 携带的 PML NB 的募集发生在病毒基因组从运输小泡中释放之后。Sp100 募集的延迟是 HPV 相关 PML NB 的特异性。这些数据表明,病毒在运输小泡在 G1 晚期破裂之前一直处于保护环境中,并暗示 HPV 可能调节 PML NB 的组装以实现感染的建立和向病毒维持的转变。