Istituto Pasteur Fondazione Cenci Bolognetti, Dipartimento di Medicina Sperimentale, Sapienza Università di Roma, Italy.
Virus Res. 2013 Aug;175(2):143-50. doi: 10.1016/j.virusres.2013.04.001. Epub 2013 Apr 23.
p29, a newly identified Kaposi's sarcoma-associated herpesvirus (KSHV) protein, is the product of ORF67, the positional homolog of the conserved herpesvirus protein UL34. Like its homologues in other herpesviruses, p29 is expressed early during viral lytic cycle, and is localized on the nuclear rim. Upon chemical induction of viral replication in primary effusion lymphoma cells, p29 interacts with p33, encoded by ORF69, the positional homolog of the conserved herpesvirus protein UL31, and both proteins colocalize on the nuclear membrane. IFA and biochemical analysis of infected or transfected cells showed that p29 expression resulted in delocalization and hyperphosphorylation of emerin, whereas other nuclear lamin associated proteins, such as LUMA, LB1 and LBR were not affected. Mislocalization of emerin was robustly increased upon combined expression of p29 and p33, suggesting that emerin destabilization might represent the first step in nuclear lamina disassembling, a process necessary for nucleocapsid maturation.
p29 是一种新鉴定的卡波氏肉瘤相关疱疹病毒 (KSHV) 蛋白,是 ORF67 的产物,ORF67 是保守疱疹病毒蛋白 UL34 的位置同源物。与其他疱疹病毒中的同源物一样,p29 在病毒裂解周期的早期表达,并定位于核边缘。在原发性渗出性淋巴瘤细胞中化学诱导病毒复制时,p29 与 ORF69 编码的 p33 相互作用,ORF69 是保守疱疹病毒蛋白 UL31 的位置同源物,这两种蛋白质都在核膜上共定位。IFA 和感染或转染细胞的生化分析表明,p29 的表达导致 emerin 的去定位和过度磷酸化,而其他核层粘连蛋白相关蛋白,如 LUMA、LB1 和 LBR 则不受影响。p29 和 p33 联合表达时,emerin 的定位错误显著增加,这表明 emerin 的不稳定可能代表核层板解组装过程的第一步,这是核衣壳成熟所必需的。