Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.
Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.
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DOI：
10.1016/j.virol.2015.12.019
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发表时间：
2016-02
期刊：
影响因子：
3.7
通讯作者：
Hutt-Fletcher LM
中科院分区：
文献类型：
--
作者：
Changotra H;Turk SM;Artigues A;Thakur N;Gore M;Muggeridge MI;Hutt-Fletcher LM
EB病毒糖蛋白复合物gMgN与完全包膜病毒的组装和释放有关，但其确切作用尚未阐明。我们在这里报告，长期预测的gM细胞质尾是不需要复杂的形成，它与细胞蛋白p32，这已被报道参与人巨细胞病毒和单纯疱疹病毒的核出口相互作用。虽然在病毒感染的细胞中没有观察到p32的再分布和与gM的共定位，但通过siRNA或慢病毒递送的shRNA敲低p32表达再现了缺乏gNgM表达的病毒的表型。从细胞中释放的一部分病毒沉积下来，具有缺乏完整包膜的病毒特征，并且被困在核浓缩染色质中的病毒有所增加。这些观察结果表明，p32也可能参与Epstein-Barr病毒的核出口。
The Epstein-Barr virus glycoprotein complex gMgN has been implicated in assembly and release of fully enveloped virus, although the precise role that it plays has not been elucidated. We report here that the long predicted cytoplasmic tail of gM is not required for complex formation and that it interacts with the cellular protein p32, which has been reported to be involved in nuclear egress of human cytomegalovirus and herpes simplex virus. Although redistribution of p32 and colocalization with gM was not observed in virus infected cells, knockdown of p32 expression by siRNA or lentivirus-delivered shRNA recapitulated the phenotype of a virus lacking expression of gNgM. A proportion of virus released from cells sedimented with characteristics of virus lacking an intact envelope and there was an increase in virus trapped in nuclear condensed chromatin. The observations suggest the possibility that p32 may also be involved in nuclear egress of Epstein-Barr virus.